Entry stringlengths 6 10 | Entry Name stringlengths 5 11 | Sequence stringlengths 2 35.2k | EC number stringlengths 7 118 ⌀ | Cofactor stringlengths 38 1.77k ⌀ | Gene Ontology (biological process) stringlengths 18 11.3k ⌀ | Gene Ontology (cellular component) stringlengths 17 1.75k ⌀ | Gene Ontology (molecular function) stringlengths 24 2.09k ⌀ | Pfam stringlengths 8 232 ⌀ | Gene3D stringlengths 10 250 ⌀ | Protein families stringlengths 9 237 ⌀ | Post-translational modification stringlengths 16 8.52k ⌀ | Subcellular location [CC] stringlengths 29 6.18k ⌀ | Catalytic activity stringlengths 64 35.7k ⌀ | Kinetics stringlengths 69 11.7k ⌀ | Pathway stringlengths 27 908 ⌀ | pH dependence stringlengths 64 955 ⌀ | Temperature dependence stringlengths 70 1.16k ⌀ | Function [CC] stringlengths 17 15.3k ⌀ | Organism stringlengths 8 196 |
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P0AFQ5 | RUTC_ECOLI | MPKSVIIPAGSSAPLAPFVPGTLADGVVYVSGTLAFDQHNNVLFADDPKAQTRHVLETIRKVIETAGGTMADVTFNSIFITDWKNYAAINEIYAEFFPGDKPARFCIQCGLVKPDALVEIATIAHIAK | 3.5.-.- | null | nitrogen utilization [GO:0019740]; organonitrogen compound catabolic process [GO:1901565]; pyrimidine nucleobase catabolic process [GO:0006208]; uracil catabolic process [GO:0006212] | cytosol [GO:0005829] | deaminase activity [GO:0019239]; identical protein binding [GO:0042802] | PF01042; | 3.30.1330.40; | RutC family | null | null | CATALYTIC ACTIVITY: Reaction=(Z)-3-aminoacrylate + H(+) + H2O = 3-oxopropanoate + NH4(+); Xref=Rhea:RHEA:34947, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:33190, ChEBI:CHEBI:59894; Evidence={ECO:0000269|PubMed:33839153}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=9.1 mM for 3-aminoacrylate {ECO:0000269|PubMed:33839153}; Note=kcat is 52 min(-1) with 3-aminoacrylate as substrate. {ECO:0000269|PubMed:33839153}; | null | null | null | FUNCTION: Involved in pyrimidine catabolism (PubMed:16540542). Catalyzes the deamination of 3-aminoacrylate to malonic semialdehyde, a reaction that can also occur spontaneously (PubMed:33839153). RutC may facilitate the reaction and modulate the metabolic fitness, rather than catalyzing essential functions (PubMed:338... | Escherichia coli (strain K12) |
P0AFR2 | DAUA_ECOLI | MNKIFSSHVMPFRALIDACWKEKYTAARFTRDLIAGITVGIIAIPLAMALAIGSGVAPQYGLYTAAVAGIVIALTGGSRFSVSGPTAAFVVILYPVSQQFGLAGLLVATLLSGIFLILMGLARFGRLIEYIPVSVTLGFTSGIGITIGTMQIKDFLGLQMAHVPEHYLQKVGALFMALPTINVGDAAIGIVTLGILVFWPRLGIRLPGHLPALLAGCAVMGIVNLLGGHVATIGSQFHYVLADGSQGNGIPQLLPQLVLPWDLPNSEFTLTWDSIRTLLPAAFSMAMLGAIESLLCAVVLDGMTGTKHKANSELVGQGLG... | null | null | aspartate transmembrane transport [GO:0015810]; fumarate transport [GO:0015741]; succinate transmembrane transport [GO:0071422] | plasma membrane [GO:0005886] | fumarate transmembrane transporter activity [GO:0015138]; L-aspartate transmembrane transporter activity [GO:0015183]; secondary active sulfate transmembrane transporter activity [GO:0008271]; succinate transmembrane transporter activity [GO:0015141] | PF01740;PF00916; | 3.30.750.24; | SLC26A/SulP transporter (TC 2.A.53) family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:23278959}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=2 H(+)(in) + succinate(in) = 2 H(+)(out) + succinate(out); Xref=Rhea:RHEA:29303, ChEBI:CHEBI:15378, ChEBI:CHEBI:30031; Evidence={ECO:0000305|PubMed:23278959}; CATALYTIC ACTIVITY: Reaction=2 H(+)(in) + L-aspartate(in) = 2 H(+)(out) + L-aspartate(out); Xref=Rhea:RHEA:29287, ChEBI:CHEBI:15378,... | null | null | null | null | FUNCTION: Responsible for the aerobic transport of succinate from the periplasm to the cytoplasm at acidic pH (PubMed:23278959). Can transport other C4-dicarboxylic acids such as aspartate and fumarate (PubMed:23278959). May also play a role in the regulation of C4-dicarboxylic acid metabolism at pH 7, via regulation o... | Escherichia coli (strain K12) |
P0AFS3 | FOLM_ECOLI | MGKTQPLPILITGGGRRIGLALAWHFINQKQPVIVSYRTHYPAIDGLINAGAQCIQADFSTNDGVMAFADEVLKSTHGLRAILHNASAWMAEKPGAPLADVLACMMQIHVNTPYLLNHALERLLRGHGHAASDIIHFTDYVVERGSDKHIAYAASKAALDNMTRSFARKLAPEVKVNSIAPSLILFNEHDDAEYRQQALNKSLMKTAPGEKEVIDLVDYLLTSCFVTGRSFPLDGGRHLR | 1.5.1.3; 1.5.1.50 | null | one-carbon metabolic process [GO:0006730]; protein homotetramerization [GO:0051289]; pteridine-containing compound biosynthetic process [GO:0042559] | null | dihydrofolate reductase activity [GO:0004146]; dihydromonapterin reductase activity [GO:0071172]; identical protein binding [GO:0042802] | PF13561; | 3.40.50.720; | Short-chain dehydrogenases/reductases (SDR) family, FolM subfamily | null | null | CATALYTIC ACTIVITY: Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000269|PubMed:14617668}; CATALYTIC ACTIVITY: Reaction=7,8-dihydromonapt... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=9.5 uM for 7,8-dihydrofolate (at pH 6.0) {ECO:0000269|PubMed:14617668}; KM=147 uM for 7,8-dihydromonapterin (at pH 6.0) {ECO:0000269|PubMed:19897652}; KM=1.9 uM for NADPH (at pH 6.0) {ECO:0000269|PubMed:14617668}; Vmax=0.083 umol/min/mg enzyme with 7,8-dihydrofolat... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 4.7. {ECO:0000269|PubMed:14617668}; | null | FUNCTION: Catalyzes the reduction of dihydromonapterin to tetrahydromonapterin. Also has lower activity with dihydrofolate. {ECO:0000269|PubMed:19897652}. | Escherichia coli (strain K12) |
P0AFS9 | MEPM_ECOLI | MQQIARSVALAFNNLPRPHRVMLGSLTVLTLAVAVWRPYVYHRDATPIVKTIELEQNEIRSLLPEASEPIDQAAQEDEAIPQDELDDKIAGEAGVHEYVVSTGDTLSSILNQYGIDMGDITQLAAADKELRNLKIGQQLSWTLTADGELQRLTWEVSRRETRTYDRTAANGFKMTSEMQQGEWVNNLLKGTVGGSFVASARNAGLTSAEVSAVIKAMQWQMDFRKLKKGDEFAVLMSREMLDGKREQSQLLGVRLRSEGKDYYAIRAEDGKFYDRNGTGLAKGFLRFPTAKQFRISSNFNPRRTNPVTGRVAPHRGVDFA... | 3.4.24.- | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:23062283}; Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:23062283}; Note=Zinc, although calcium also allows some activity. {ECO:0000269|PubMed:23062283}; | capsule polysaccharide biosynthetic process [GO:0045227]; cell wall organization [GO:0071555]; peptidoglycan metabolic process [GO:0000270]; peptidoglycan turnover [GO:0009254]; proteolysis [GO:0006508]; septum digestion after cytokinesis [GO:0000920] | plasma membrane [GO:0005886] | endopeptidase activity [GO:0004175]; metal ion binding [GO:0046872]; metalloendopeptidase activity [GO:0004222] | PF19425;PF01476;PF08525;PF01551; | 3.10.450.350;2.70.70.10; | Peptidase M23B family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Note=Uniform peripheral location, with partial enrichment at cell poles. | null | null | PATHWAY: Cell wall biogenesis; cell wall polysaccharide biosynthesis. | null | null | FUNCTION: A murein DD-endopeptidase with specificity for D-Ala-meso-diaminopimelic acid (mDAP) cross-links. Its role is probably to cleave D-Ala-mDAP cross-links to allow insertion of new glycans and thus cell wall expansion. Functionally redundant with MepM and MepH. Partially suppresses an mepS disruption mutant. {EC... | Escherichia coli (strain K12) |
P0AFT2 | TCYL_ECOLI | MQESIQLVIDSLPFLLKGAGYTLQLSIGGMFFGLLLGFILALMRLSPIWPVRWLARFYISIFRGTPLIAQLFMIYYGLPQFGIELDPIPSAMIGLSLNTAAYAAETLRAAISSIDKGQWEAAASIGMTPWQTMRRAILPQAARVALPPLSNSFISLVKDTSLAATIQVPELFRQAQLITSRTLEVFTMYLAASLIYWIMATVLSTLQNHFENQLNRQEREPK | null | null | cysteine transmembrane transport [GO:1903712]; L-cystine transport [GO:0015811]; sulfur utilization [GO:0006791] | ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing [GO:0055052]; plasma membrane [GO:0005886] | L-cystine transmembrane transporter activity [GO:0015184] | PF00528; | 1.10.3720.10; | Binding-protein-dependent transport system permease family, HisMQ subfamily | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: Part of the ABC transporter complex TcyJLN involved in L-cystine import (PubMed:20351115, PubMed:25139244, PubMed:25837721, PubMed:26350134). This high affinity cystine transporter is involved in resistance to oxidative stress by forming a L-cysteine/L-cystine shuttle system with the EamA transporter, which e... | Escherichia coli (strain K12) |
P0AFU4 | GLRR_ECOLI | MSHKPAHLLLVDDDPGLLKLLGLRLTSEGYSVVTAESGAEGLRVLNREKVDLVISDLRMDEMDGMQLFAEIQKVQPGMPVIILTAHGSIPDAVAATQQGVFSFLTKPVDKDALYQAIDDALEQSAPATDERWREAIVTRSPLMLRLLEQARLVAQSDVSVLINGQSGTGKEIFAQAIHNASPRNSKPFIAINCGALPEQLLESELFGHARGAFTGAVSNREGLFQAAEGGTLFLDEIGDMPAPLQVKLLRVLQERKVRPLGSNRDIDINVRIISATHRDLPKAMARGEFREDLYYRLNVVSLKIPALAERTEDIPLLANH... | null | null | DNA-templated transcription [GO:0006351]; phosphorelay signal transduction system [GO:0000160]; positive regulation of DNA-templated transcription [GO:0045893] | cytoplasm [GO:0005737] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; cis-regulatory region sequence-specific DNA binding [GO:0000987]; DNA-binding transcription factor activity [GO:0003700]; phosphorelay response regulator activity [GO:0000156] | PF00072;PF00158; | 1.10.8.60;3.40.50.2300;1.10.10.60;3.40.50.300; | null | PTM: Phosphorylated by GlrK. {ECO:0000269|PubMed:15522865}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. | null | null | null | null | null | FUNCTION: Member of the two-component regulatory system GlrR/GlrK that up-regulates transcription of the glmY sRNA when cells enter the stationary growth phase. Regulates glmY transcription by binding to three conserved sites in the purL-glmY intergenic region. {ECO:0000269|PubMed:19843219}. | Escherichia coli (strain K12) |
P0AFV4 | MEPS_ECOLI | MVKSQPILRYILRGIPAIAVAVLLSACSANNTAKNMHPETRAVGSETSSLQASQDEFENLVRNVDVKSRIMDQYADWKGVRYRLGGSTKKGIDCSGFVQRTFREQFGLELPRSTYEQQEMGKSVSRSNLRTGDLVLFRAGSTGRHVGIYIGNNQFVHASTSSGVIISSMNEPYWKKRYNEARRVLSRS | 3.4.-.-; 3.4.17.13 | null | capsule polysaccharide biosynthetic process [GO:0045227]; cell wall organization [GO:0071555]; peptidoglycan metabolic process [GO:0000270]; peptidoglycan turnover [GO:0009254]; proteolysis [GO:0006508] | cell outer membrane [GO:0009279] | cysteine-type peptidase activity [GO:0008234]; endopeptidase activity [GO:0004175]; muramoyltetrapeptide carboxypeptidase activity [GO:0106415] | PF00877; | 3.90.1720.10; | Peptidase C40 family | null | SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000305}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303}. | CATALYTIC ACTIVITY: Reaction=H2O + N-acetyl-D-glucosaminyl-N-acetylmuramoyl-L-alanyl-D-glutamyl-6-carboxy-L-lysyl-D-alanine = D-alanine + N-acetyl-D-glucosaminyl-N-acetylmuramoyl-L-alanyl-D-glutamyl-6-carboxy-L-lysyl; Xref=Rhea:RHEA:48688, ChEBI:CHEBI:15377, ChEBI:CHEBI:57416, ChEBI:CHEBI:90762, ChEBI:CHEBI:90763; EC=3... | null | PATHWAY: Cell wall biogenesis; cell wall polysaccharide biosynthesis. | null | null | FUNCTION: A murein DD-endopeptidase with specificity for D-Ala-meso-diaminopimelic acid (mDAP) cross-links. Its role is probably to cleave D-Ala-mDAP cross-links to allow insertion of new glycans and thus cell wall expansion. Functionally redundant with MepM and MepH. Also has weak LD-carboxypeptidase activity on L-mDA... | Escherichia coli (strain K12) |
P0AFW0 | RFAH_ECOLI | MQSWYLLYCKRGQLQRAQEHLERQAVNCLAPMITLEKIVRGKRTAVSEPLFPNYLFVEFDPEVIHTTTINATRGVSHFVRFGASPAIVPSAVIHQLSVYKPKDIVDPATPYPGDKVIITEGAFEGFQAIFTEPDGEARSMLLLNLINKEIKHSVKNTEFRKL | null | null | DNA-templated transcription elongation [GO:0006354]; positive regulation of translation [GO:0045727]; transcription antitermination [GO:0031564]; transcription elongation-coupled chromatin remodeling [GO:0140673] | cytosol [GO:0005829] | bacterial-type RNA polymerase core enzyme binding [GO:0001000]; DNA binding [GO:0003677]; regulatory RNA binding [GO:0061980]; transcription antitermination factor activity, DNA binding [GO:0001073]; translation activator activity [GO:0008494] | PF02357; | 3.30.70.940; | RfaH family | null | null | null | null | null | null | null | FUNCTION: Enhances distal genes transcription elongation in a specialized subset of operons that encode extracytoplasmic components. RfaH is recruited into a multi-component RNA polymerase complex by the ops element, which is a short conserved DNA sequence located downstream of the main promoter of these operons. Once ... | Escherichia coli (strain K12) |
P0AFX0 | HPF_ECOLI | MQLNITGNNVEITEALREFVTAKFAKLEQYFDRINQVYVVLKVEKVTHTSDATLHVNGGEIHASAEGQDMYAAIDGLIDKLARQLTKHKDKLKQH | null | null | dormancy process [GO:0022611]; negative regulation of translation [GO:0017148]; negative regulation of translational elongation [GO:0045900] | cytosol [GO:0005829]; cytosolic small ribosomal subunit [GO:0022627] | ribosomal small subunit binding [GO:0043024]; ribosome binding [GO:0043022] | PF02482; | 3.30.160.100; | HPF/YfiA ribosome-associated protein family, Short HPF subfamily | null | null | null | null | null | null | null | FUNCTION: During stationary phase, promotes and stabilizes dimerization of 70S ribosomes by the ribosome modulation factor (RMF), leading to the formation of inactive 100S ribosomes (PubMed:18174192). Converts immature 90S particles formed by RMF into 100S ribosomes (PubMed:16324148). Crystallization with T.thermophilu... | Escherichia coli (strain K12) |
P0AFX7 | RSEA_ECOLI | MQKEQLSALMDGETLDSELLNELAHNPEMQKTWESYHLIRDSMRGDTPEVLHFDISSRVMAAIEEEPVRQPATLIPEAQPAPHQWQKMPFWQKVRPWAAQLTQMGVAACVSLAVIVGVQHYNGQSETSQQPETPVFNTLPMMGKASPVSLGVPSEATANNGQQQQVQEQRRRINAMLQDYELQRRLHSEQLQFEQAQTQQAAVQVPGIQTLGTQSQ | null | null | negative regulation of DNA-templated transcription [GO:0045892] | plasma membrane [GO:0005886]; sigma factor antagonist complex [GO:1903865] | molecular adaptor activity [GO:0060090]; sigma factor antagonist activity [GO:0016989] | PF03873;PF03872; | 1.20.5.3960;1.10.10.880; | RseA family | PTM: Sequentially cleaved by DegS (a site-1 protease) in its periplasmic domain between Val-148 and Ser-149, then by RseP (a site-2 protease) between positions Ala-108 and Cys-109. The N-terminal fragment is then degraded by primarily ClpX-ClpP in an ATP-dependent fashion. Sequential cleavage by DegS, RseP and ClpX-Clp... | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:11777003, ECO:0000269|PubMed:12183369, ECO:0000269|PubMed:9159522, ECO:0000269|PubMed:9159523}; Single-pass type II membrane protein {ECO:0000269|PubMed:11777003, ECO:0000269|PubMed:12183369, ECO:0000269|PubMed:9159522, ECO:0000269|PubMed:9159523}. Note=Foll... | null | null | null | null | null | FUNCTION: An anti-sigma factor for extracytoplasmic function (ECF) sigma factor sigma-E (RpoE). ECF sigma factors are held in an inactive form by an anti-sigma factor until released by regulated intramembrane proteolysis (RIP). RIP occurs when an extracytoplasmic signal triggers a concerted proteolytic cascade to trans... | Escherichia coli (strain K12) |
P0AFX9 | RSEB_ECOLI | MKQLWFAMSLVTGSLLFSANASATPASGALLQQMNLASQSLNYELSFISINKQGVESLRYRHARLDNRPLAQLLQMDGPRREVVQRGNEISYFEPGLEPFTLNGDYIVDSLPSLIYTDFKRLSPYYDFISVGRTRIADRLCEVIRVVARDGTRYSYIVWMDTESKLPMRVDLLDRDGETLEQFRVIAFNVNQDISSSMQTLAKANLPPLLSVPVGEKAKFSWTPTWLPQGFSEVSSSRRPLPTMDNMPIESRLYSDGLFSFSVNVNRATPSSTDQMLRTGRRTVSTSVRDNAEITIVGELPPQTAKRIAENIKFGAAQ | null | null | negative regulation of DNA-templated transcription [GO:0045892]; protein stabilization [GO:0050821]; regulation of polysaccharide biosynthetic process [GO:0032885] | outer membrane-bounded periplasmic space [GO:0030288]; plasma membrane [GO:0005886]; sigma factor antagonist complex [GO:1903865] | antisigma factor binding [GO:0045152]; identical protein binding [GO:0042802]; lipid binding [GO:0008289] | PF03888;PF17188; | 2.50.20.10;3.30.200.100; | RseB family | null | SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:11777003, ECO:0000269|PubMed:9159522, ECO:0000269|PubMed:9159523}. Note=Partially associates with the inner membrane via RseA. | null | null | null | null | null | FUNCTION: Negatively modulates the activity of sigma-E (RpoE) by stabilizing RseA under non-stress conditions. Although not essential for association of sigma-E with Rsea it increases their affinity 2- to 3-fold. When bound to RseA it prevents proteolysis by DegS, which is probably relieved by lipopolysaccharide bindin... | Escherichia coli (strain K12) |
P0AFY6 | SBMA_ECOLI | MFKSFFPKPGTFFLSAFVWALIAVIFWQAGGGDWVARITGASGQIPISAARFWSLDFLIFYAYYIVCVGLFALFWFIYSPHRWQYWSILGTALIIFVTWFLVEVGVAVNAWYAPFYDLIQTALSSPHKVTIEQFYREVGVFLGIALIAVVISVLNNFFVSHYVFRWRTAMNEYYMANWQQLRHIEGAAQRVQEDTMRFASTLENMGVSFINAIMTLIAFLPVLVTLSAHVPELPIIGHIPYGLVIAAIVWSLMGTGLLAVVGIKLPGLEFKNQRVEAAYRKELVYGEDDATRATPPTVRELFSAVRKNYFRLYFHYMYFN... | null | null | fatty acid beta-oxidation [GO:0006635]; long-chain fatty acid import into peroxisome [GO:0015910]; microcin B17 transport [GO:0042885]; microcin transport [GO:0042884]; peptide transport [GO:0015833]; peroxisome organization [GO:0007031]; protein transport [GO:0015031]; response to antibiotic [GO:0046677]; toxin transp... | peroxisomal membrane [GO:0005778]; plasma membrane [GO:0005886] | ATP binding [GO:0005524]; ATPase-coupled transmembrane transporter activity [GO:0042626]; long-chain fatty acid transporter activity [GO:0005324]; microcin transmembrane transporter activity [GO:0015638]; peptide transmembrane transporter activity [GO:1904680]; protein homodimerization activity [GO:0042803]; secondary ... | PF05992; | null | Peptide uptake permease (PUP) (TC 9.A.18) family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000269|PubMed:15919996}. | null | null | null | null | null | FUNCTION: Uptake of antimicrobial peptides. Required for the transport of microcin B17 (MccB17), microcin 25 (Mcc25) and proline-rich antimicrobial peptides (such as Cathelicidin-3, Arasin 1 and Dro/Drosocin) into the cell. {ECO:0000269|PubMed:17725560, ECO:0000269|PubMed:3543211, ECO:0000269|PubMed:36997646, ECO:00002... | Escherichia coli (strain K12) |
P0AFY8 | SEQA_ECOLI | MKTIEVDDELYSYIASHTKHIGESASDILRRMLKFSAASQPAAPVTKEVRVASPAIVEAKPVKTIKDKVRAMRELLLSDEYAEQKRAVNRFMLLLSTLYSLDAQAFAEATESLHGRTRVYFAADEQTLLKNGNQTKPKHVPGTPYWVITNTNTGRKCSMIEHIMQSMQFPAELIEKVCGTI | null | null | negative regulation of DNA-templated DNA replication initiation [GO:0032297]; nucleoid organization [GO:0090143]; regulation of DNA-templated transcription [GO:0006355]; response to radiation [GO:0009314]; sister chromatid cohesion [GO:0007062] | cytosol [GO:0005829]; protein-containing complex [GO:0032991]; SeqA-DNA complex [GO:1990097] | DNA replication origin binding [GO:0003688]; double-stranded methylated DNA binding [GO:0010385]; hemi-methylated DNA-binding [GO:0044729]; identical protein binding [GO:0042802]; protein homodimerization activity [GO:0042803] | PF03925;PF17206; | 1.10.1220.10;1.20.1380.10; | SeqA family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00908, ECO:0000269|PubMed:9660922}. Note=Localization is cell cycle-dependent. Localizes at midcell in newborn cells, then migrates in opposite directions toward cell quarter sites and remains tethered there until the cell divides. | null | null | null | null | null | FUNCTION: Negative regulator of replication initiation, which contributes to regulation of DNA replication and ensures that replication initiation occurs exactly once per chromosome per cell cycle. Binds to pairs of hemimethylated GATC sequences in the oriC region, thus preventing assembly of replication proteins and r... | Escherichia coli (strain K12) |
P0AFZ3 | SSPB_ECOLI | MDLSQLTPRRPYLLRAFYEWLLDNQLTPHLVVDVTLPGVQVPMEYARDGQIVLNIAPRAVGNLELANDEVRFNARFGGIPRQVSVPLAAVLAIYARENGAGTMFEPEAAYDEDTSIMNDEEASADNETVMSVIDGDKPDHDDDTHPDDEPPQPPRGGRPALRVVK | null | null | positive regulation of ATP-dependent activity [GO:0032781]; positive regulation of protein catabolic process [GO:0045732]; positive regulation of proteolysis involved in protein catabolic process [GO:1903052] | cytosol [GO:0005829]; HslUV protease complex [GO:0009376]; ribosome [GO:0005840] | ATPase binding [GO:0051117]; molecular adaptor activity [GO:0060090]; protein homodimerization activity [GO:0042803]; RNA binding [GO:0003723] | PF04386; | 2.30.30.220; | SspB family | null | null | null | null | null | null | null | FUNCTION: Enhances recognition of ssrA-tagged proteins by the ClpX-ClpP protease; the ssrA degradation tag (AANDENYALAA) is added trans-translationally to proteins that are stalled on the ribosome, freeing the ribosome and targeting stalled peptides for degradation. SspB activates the ATPase activity of ClpX. Seems to ... | Escherichia coli (strain K12) |
P0AFZ5 | SULA_ECOLI | MYTSGYAHRSSSFSSAASKIARVSTENTTAGLISEVVYREDQPMMTQLLLLPLLQQLGQQSRWQLWLTPQQKLSREWVQASGLPLTKVMQISQLSPCHTVESMVRALRTGNYSVVIGWLADDLTEEEHAELVDAANEGNAMGFIMRPVSASSHATRQLSGLKIHSNLYH | null | null | division septum assembly [GO:0000917]; DNA damage response [GO:0006974]; negative regulation of cell division [GO:0051782]; negative regulation of cytokinesis [GO:0032466]; negative regulation of FtsZ-dependent cytokinesis [GO:2000245]; negative regulation of protein polymerization [GO:0032272]; SOS response [GO:000943... | null | null | PF03846; | 3.40.50.300; | SulA family | PTM: Is rapidly cleaved and degraded by the Lon protease once DNA damage is repaired. {ECO:0000269|PubMed:10788793, ECO:0000269|PubMed:11513747, ECO:0000269|PubMed:6300834, ECO:0000269|PubMed:9180687}. | null | null | null | null | null | null | FUNCTION: Component of the SOS system and an inhibitor of cell division. Accumulation of SulA causes rapid cessation of cell division and the appearance of long, non-septate filaments. In the presence of GTP, binds a polymerization-competent form of FtsZ in a 1:1 ratio, thus inhibiting FtsZ polymerization and therefore... | Escherichia coli (strain K12) |
P0AG07 | RPE_ECOLI | MKQYLIAPSILSADFARLGEDTAKALAAGADVVHFDVMDNHYVPNLTIGPMVLKSLRNYGITAPIDVHLMVKPVDRIVPDFAAAGASIITFHPEASEHVDRTLQLIKENGCKAGLVFNPATPLSYLDYVMDKLDVILLMSVNPGFGGQSFIPQTLDKLREVRRRIDESGFDIRLEVDGGVKVNNIGEIAAAGADMFVAGSAIFDQPDYKKVIDEMRSELAKVSHE | 5.1.3.1 | COFACTOR: Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000269|PubMed:21402925}; Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000269|PubMed:21402925}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:21402925}; Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:21402925}; No... | pentose catabolic process [GO:0019323]; pentose-phosphate shunt, non-oxidative branch [GO:0009052] | cytosol [GO:0005829] | D-ribulose-phosphate 3-epimerase activity [GO:0004750]; ferrous iron binding [GO:0008198]; metal ion binding [GO:0046872] | PF00834; | 3.20.20.70; | Ribulose-phosphate 3-epimerase family | null | null | CATALYTIC ACTIVITY: Reaction=D-ribulose 5-phosphate = D-xylulose 5-phosphate; Xref=Rhea:RHEA:13677, ChEBI:CHEBI:57737, ChEBI:CHEBI:58121; EC=5.1.3.1; Evidence={ECO:0000255|HAMAP-Rule:MF_02227, ECO:0000269|PubMed:21402925}; | null | PATHWAY: Carbohydrate degradation. {ECO:0000255|HAMAP-Rule:MF_02227, ECO:0000269|PubMed:21402925}. | null | null | FUNCTION: Catalyzes the reversible epimerization of D-ribulose 5-phosphate to D-xylulose 5-phosphate. {ECO:0000255|HAMAP-Rule:MF_02227, ECO:0000269|PubMed:21402925}. | Escherichia coli (strain K12) |
P0AG11 | UMUD_ECOLI | MLFIKPADLREIVTFPLFSDLVQCGFPSPAADYVEQRIDLNQLLIQHPSATYFVKASGDSMIDGGISDGDLLIVDSAITASHGDIVIAAVDGEFTVKKLQLRPTVQLIPMNSAYSPITISSEDTLDVFGVVIHVVKAMR | 3.4.21.- | null | DNA damage response [GO:0006974]; DNA repair [GO:0006281]; proteolysis [GO:0006508]; regulation of DNA-templated transcription [GO:0006355]; SOS response [GO:0009432]; translesion synthesis [GO:0019985] | DNA polymerase V complex [GO:0009355] | ATP-dependent activity, acting on DNA [GO:0008094]; DNA-directed DNA polymerase activity [GO:0003887]; identical protein binding [GO:0042802]; nucleic acid binding [GO:0003676]; serine-type peptidase activity [GO:0008236]; single-stranded DNA binding [GO:0003697] | PF00717; | 2.10.109.10; | Peptidase S24 family | null | null | null | null | null | null | null | FUNCTION: Involved in UV protection and mutation. Poorly processive, error-prone DNA polymerase involved in translesion repair (PubMed:10801133). Essential for induced (or SOS) mutagenesis. Able to replicate DNA across DNA lesions (thymine photodimers and abasic sites, called translesion synthesis) in the presence of a... | Escherichia coli (strain K12) |
P0AG16 | PUR1_ECOLI | MCGIVGIAGVMPVNQSIYDALTVLQHRGQDAAGIITIDANNCFRLRKANGLVSDVFEARHMQRLQGNMGIGHVRYPTAGSSSASEAQPFYVNSPYGITLAHNGNLTNAHELRKKLFEEKRRHINTTSDSEILLNIFASELDNFRHYPLEADNIFAAIAATNRLIRGAYACVAMIIGHGMVAFRDPNGIRPLVLGKRDIDENRTEYMVASESVALDTLGFDFLRDVAPGEAIYITEEGQLFTRQCADNPVSNPCLFEYVYFARPDSFIDKISVYSARVNMGTKLGEKIAREWEDLDIDVVIPIPETSCDIALEIARILGKP... | 2.4.2.14 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_01931}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01931}; | 'de novo' IMP biosynthetic process [GO:0006189]; glutamine metabolic process [GO:0006541]; purine nucleobase biosynthetic process [GO:0009113]; purine nucleotide biosynthetic process [GO:0006164] | cytoplasm [GO:0005737]; cytosol [GO:0005829] | amidophosphoribosyltransferase activity [GO:0004044]; glycosyltransferase activity [GO:0016757]; guanosine tetraphosphate binding [GO:0097216]; identical protein binding [GO:0042802]; magnesium ion binding [GO:0000287] | PF13522;PF00156; | 3.40.50.2020;3.60.20.10; | Purine/pyrimidine phosphoribosyltransferase family | null | null | CATALYTIC ACTIVITY: Reaction=5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = 5-phospho-alpha-D-ribose 1-diphosphate + H2O + L-glutamine; Xref=Rhea:RHEA:14905, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:33019, ChEBI:CHEBI:58017, ChEBI:CHEBI:58359, ChEBI:CHEBI:58681; EC=2.4.2.14; Evidence={ECO:0000255|... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.067 mM for phosphoribosylpyrophosphate {ECO:0000269|PubMed:372191}; KM=1.7 mM for glutamine {ECO:0000269|PubMed:372191}; KM=8.8 mM for NH(3) {ECO:0000269|PubMed:372191}; | PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/2. {ECO:0000255|HAMAP-Rule:MF_01931, ECO:0000269|PubMed:372191}. | null | null | FUNCTION: Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine. Can also use NH(3) in place of glutamine. {ECO:0000269|PubMed:372191}. | Escherichia coli (strain K12) |
P0AG18 | PURE_ECOLI | MSSRNNPARVAIVMGSKSDWATMQFAAEIFEILNVPHHVEVVSAHRTPDKLFSFAESAEENGYQVIIAGAGGAAHLPGMIAAKTLVPVLGVPVQSAALSGVDSLYSIVQMPRGIPVGTLAIGKAGAANAALLAAQILATHDKELHQRLNDWRKAQTDEVLENPDPRGAA | 5.4.99.18 | null | 'de novo' IMP biosynthetic process [GO:0006189] | cytosol [GO:0005829] | 5-(carboxyamino)imidazole ribonucleotide mutase activity [GO:0034023]; identical protein binding [GO:0042802] | PF00731; | 3.40.50.1970; | AIR carboxylase family, Class I subfamily | null | null | CATALYTIC ACTIVITY: Reaction=5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole + H(+) = 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate; Xref=Rhea:RHEA:13193, ChEBI:CHEBI:15378, ChEBI:CHEBI:58730, ChEBI:CHEBI:77657; EC=5.4.99.18; Evidence={ECO:0000255|HAMAP-Rule:MF_01929, ECO:0000269|PubMed:10074353, ECO:0000269|P... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=140 uM for N5-CAIR {ECO:0000269|PubMed:8117684}; | PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate from 5-amino-1-(5-phospho-D-ribosyl)imidazole (N5-CAIR route): step 2/2. {ECO:0000255|HAMAP-Rule:MF_01929, ECO:0000269|PubMed:8117684}. | null | null | FUNCTION: Catalyzes the conversion of N5-carboxyaminoimidazole ribonucleotide (N5-CAIR) to 4-carboxy-5-aminoimidazole ribonucleotide (CAIR). {ECO:0000255|HAMAP-Rule:MF_01929, ECO:0000269|PubMed:8117684}. | Escherichia coli (strain K12) |
P0AG20 | RELA_ECOLI | MVAVRSAHINKAGEFDPEKWIASLGITSQKSCECLAETWAYCLQQTQGHPDASLLLWRGVEMVEILSTLSMDIDTLRAALLFPLADANVVSEDVLRESVGKSVVNLIHGVRDMAAIRQLKATHTDSVSSEQVDNVRRMLLAMVDDFRCVVIKLAERIAHLREVKDAPEDERVLAAKECTNIYAPLANRLGIGQLKWELEDYCFRYLHPTEYKRIAKLLHERRLDREHYIEEFVGHLRAEMKAEGVKAEVYGRPKHIYSIWRKMQKKNLAFDELFDVRAVRIVAERLQDCYAALGIVHTHYRHLPDEFDDYVANPKPNGYQ... | 2.7.6.5 | null | guanosine tetraphosphate biosynthetic process [GO:0015970]; guanosine tetraphosphate metabolic process [GO:0015969]; nucleobase-containing small molecule interconversion [GO:0015949]; phosphorylation [GO:0016310]; response to starvation [GO:0042594] | plasma membrane [GO:0005886] | ATP binding [GO:0005524]; GTP binding [GO:0005525]; GTP diphosphokinase activity [GO:0008728]; guanosine-3',5'-bis(diphosphate) 3'-diphosphatase activity [GO:0008893]; kinase activity [GO:0016301] | PF13291;PF13328;PF19296;PF04607;PF02824; | 3.10.20.30;3.30.70.260;3.30.460.10;1.10.3210.10; | RelA/SpoT family | null | null | CATALYTIC ACTIVITY: Reaction=ATP + GTP = AMP + guanosine 3'-diphosphate 5'-triphosphate; Xref=Rhea:RHEA:22088, ChEBI:CHEBI:30616, ChEBI:CHEBI:37565, ChEBI:CHEBI:142410, ChEBI:CHEBI:456215; EC=2.7.6.5; | null | PATHWAY: Purine metabolism; ppGpp biosynthesis; ppGpp from GTP: step 1/2. | null | null | FUNCTION: In eubacteria ppGpp (guanosine 3'-diphosphate 5'-diphosphate) is a mediator of the stringent response which coordinates a variety of cellular activities in response to changes in nutritional abundance. This enzyme catalyzes the formation of pppGpp which is then hydrolyzed to form ppGpp. The second messengers ... | Escherichia coli (strain K12) |
P0AG24 | SPOT_ECOLI | MYLFESLNQLIQTYLPEDQIKRLRQAYLVARDAHEGQTRSSGEPYITHPVAVACILAEMKLDYETLMAALLHDVIEDTPATYQDMEQLFGKSVAELVEGVSKLDKLKFRDKKEAQAENFRKMIMAMVQDIRVILIKLADRTHNMRTLGSLRPDKRRRIARETLEIYSPLAHRLGIHHIKTELEELGFEALYPNRYRVIKEVVKAARGNRKEMIQKILSEIEGRLQEAGIPCRVSGREKHLYSIYCKMVLKEQRFHSIMDIYAFRVIVNDSDTCYRVLGQMHSLYKPRPGRVKDYIAIPKANGYQSLHTSMIGPHGVPVEV... | 2.7.6.5; 3.1.7.2 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; | guanosine tetraphosphate biosynthetic process [GO:0015970]; guanosine tetraphosphate metabolic process [GO:0015969]; nucleobase-containing small molecule interconversion [GO:0015949]; phosphorylation [GO:0016310]; response to starvation [GO:0042594] | cytosol [GO:0005829]; plasma membrane [GO:0005886] | GTP diphosphokinase activity [GO:0008728]; guanosine-3',5'-bis(diphosphate) 3'-diphosphatase activity [GO:0008893]; kinase activity [GO:0016301] | PF13291;PF13328;PF19296;PF04607;PF02824; | 3.10.20.30;3.30.70.260;3.30.460.10;1.10.3210.10; | RelA/SpoT family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17616600}. Note=Is associated with pre-50S ribosomal subunits in a salt-dependent manner. | CATALYTIC ACTIVITY: Reaction=ATP + GTP = AMP + guanosine 3'-diphosphate 5'-triphosphate; Xref=Rhea:RHEA:22088, ChEBI:CHEBI:30616, ChEBI:CHEBI:37565, ChEBI:CHEBI:142410, ChEBI:CHEBI:456215; EC=2.7.6.5; CATALYTIC ACTIVITY: Reaction=guanosine 3',5'-bis(diphosphate) + H2O = diphosphate + GDP + H(+); Xref=Rhea:RHEA:14253, C... | null | PATHWAY: Purine metabolism; ppGpp biosynthesis; ppGpp from GDP: step 1/1.; PATHWAY: Purine metabolism; ppGpp biosynthesis; ppGpp from GTP: step 1/2. | null | null | FUNCTION: In eubacteria ppGpp (guanosine 3'-diphosphate 5'-diphosphate) is a mediator of the stringent response which coordinates a variety of cellular activities in response to changes in nutritional abundance. This enzyme catalyzes both the synthesis and degradation of ppGpp. The second messengers ppGpp and c-di-GMP ... | Escherichia coli (strain K12) |
P0AG30 | RHO_ECOLI | MNLTELKNTPVSELITLGENMGLENLARMRKQDIIFAILKQHAKSGEDIFGDGVLEILQDGFGFLRSADSSYLAGPDDIYVSPSQIRRFNLRTGDTISGKIRPPKEGERYFALLKVNEVNFDKPENARNKILFENLTPLHANSRLRMERGNGSTEDLTARVLDLASPIGRGQRGLIVAPPKAGKTMLLQNIAQSIAYNHPDCVLMVLLIDERPEEVTEMQRLVKGEVVASTFDEPASRHVQVAEMVIEKAKRLVEHKKDVIILLDSITRLARAYNTVVPASGKVLTGGVDANALHRPKRFFGAARNVEEGGSLTIIATAL... | 3.6.4.- | null | DNA-templated transcription termination [GO:0006353] | cytosol [GO:0005829]; membrane [GO:0016020] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent activity, acting on RNA [GO:0008186]; helicase activity [GO:0004386]; identical protein binding [GO:0042802]; RNA binding [GO:0003723] | PF00006;PF07498;PF07497; | 1.10.720.10;2.40.50.140;3.40.50.300; | Rho family | null | null | null | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=11 uM for ATP {ECO:0000269|PubMed:7487110}; | null | null | null | FUNCTION: Facilitates transcription termination by a mechanism that involves Rho binding to the nascent RNA, activation of Rho's RNA-dependent ATPase activity, and release of the mRNA from the DNA template. RNA-dependent NTPase which utilizes all four ribonucleoside triphosphates as substrates. {ECO:0000269|PubMed:1716... | Escherichia coli (strain K12) |
P0AG55 | RL6_ECOLI | MSRVAKAPVVVPAGVDVKINGQVITIKGKNGELTRTLNDAVEVKHADNTLTFGPRDGYADGWAQAGTARALLNSMVIGVTEGFTKKLQLVGVGYRAAVKGNVINLSLGFSHPVDHQLPAGITAECPTQTEIVLKGADKQVIGQVAADLRAYRRPEPYKGKGVRYADEVVRTKEAKKK | null | null | cytoplasmic translation [GO:0002181]; response to antibiotic [GO:0046677]; ribosomal large subunit assembly [GO:0000027] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; cytosolic large ribosomal subunit [GO:0022625] | large ribosomal subunit rRNA binding [GO:0070180]; structural constituent of ribosome [GO:0003735] | PF00347; | 3.90.930.12; | Universal ribosomal protein uL6 family | null | null | null | null | null | null | null | FUNCTION: This protein binds directly to at least 2 domains of the 23S ribosomal RNA, thus is important in its secondary structure. It is located near the subunit interface in the base of the L7/L12 stalk, and near the tRNA binding site of the peptidyltransferase center. {ECO:0000269|PubMed:6170935}.; FUNCTION: Gentami... | Escherichia coli (strain K12) |
P0AG59 | RS14_ECOLI | MAKQSMKAREVKRVALADKYFAKRAELKAIISDVNASDEDRWNAVLKLQTLPRDSSPSRQRNRCRQTGRPHGFLRKFGLSRIKVREAAMRGEIPGLKKASW | null | null | cytoplasmic translation [GO:0002181]; ribosomal small subunit assembly [GO:0000028]; translation [GO:0006412] | cytoplasm [GO:0005737]; cytosolic small ribosomal subunit [GO:0022627]; small ribosomal subunit [GO:0015935] | rRNA binding [GO:0019843]; structural constituent of ribosome [GO:0003735]; tRNA binding [GO:0000049] | PF00253; | 1.10.287.1480; | Universal ribosomal protein uS14 family | null | null | null | null | null | null | null | FUNCTION: Binds 16S rRNA, required for the assembly of 30S particles and may also be responsible for determining the conformation of the 16S rRNA at the A site. | Escherichia coli (strain K12) |
P0AG63 | RS17_ECOLI | MTDKIRTLQGRVVSDKMEKSIVVAIERFVKHPIYGKFIKRTTKLHVHDENNECGIGDVVEIRECRPLSKTKSWTLVRVVEKAVL | null | null | cytoplasmic translation [GO:0002181]; response to antibiotic [GO:0046677]; ribosomal small subunit assembly [GO:0000028] | cytoplasm [GO:0005737]; cytosolic small ribosomal subunit [GO:0022627] | molecular adaptor activity [GO:0060090]; rRNA binding [GO:0019843]; small ribosomal subunit rRNA binding [GO:0070181]; structural constituent of ribosome [GO:0003735]; zinc ion binding [GO:0008270] | PF00366; | 2.40.50.140; | Universal ribosomal protein uS17 family | null | null | null | null | null | null | null | FUNCTION: One of the primary rRNA binding proteins, it binds specifically to the 5'-end of 16S ribosomal RNA (PubMed:4598121). Also plays a role in translational accuracy; neamine-resistant ribosomes show reduced neamine-induced misreading in vitro (PubMed:765484, PubMed:781296). {ECO:0000269|PubMed:4598121, ECO:000026... | Escherichia coli (strain K12) |
P0AG67 | RS1_ECOLI | MTESFAQLFEESLKEIETRPGSIVRGVVVAIDKDVVLVDAGLKSESAIPAEQFKNAQGELEIQVGDEVDVALDAVEDGFGETLLSREKAKRHEAWITLEKAYEDAETVTGVINGKVKGGFTVELNGIRAFLPGSLVDVRPVRDTLHLEGKELEFKVIKLDQKRNNVVVSRRAVIESENSAERDQLLENLQEGMEVKGIVKNLTDYGAFVDLGGVDGLLHITDMAWKRVKHPSEIVNVGDEITVKVLKFDRERTRVSLGLKQLGEDPWVAIAKRYPEGTKLTGRVTNLTDYGCFVEIEEGVEGLVHVSEMDWTNKNIHPSK... | null | null | cytoplasmic translation [GO:0002181]; negative regulation of cytoplasmic translation [GO:2000766]; positive regulation of cytoplasmic translation [GO:2000767]; ribosomal small subunit assembly [GO:0000028]; RNA secondary structure unwinding [GO:0010501]; translation [GO:0006412] | cytoplasm [GO:0005737]; cytosolic small ribosomal subunit [GO:0022627]; membrane [GO:0016020] | mRNA binding [GO:0003729]; RNA binding [GO:0003723]; single-stranded RNA binding [GO:0003727]; structural constituent of ribosome [GO:0003735] | PF00575; | 2.40.50.140; | Bacterial ribosomal protein bS1 family | PTM: Phosphorylated; probably on a serine. {ECO:0000269|PubMed:7783627}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:342903}. | null | null | null | null | null | FUNCTION: Required for translation of most natural mRNAs except for leaderless mRNA (PubMed:12068815, PubMed:17376482, PubMed:24339747, PubMed:7003157, PubMed:9677288). Binds mRNA upstream of the Shine-Dalgarno (SD) sequence and helps it bind to the 30S ribosomal subunit; acts as an RNA chaperone to unfold structured m... | Escherichia coli (strain K12) |
P0AG74 | RUSA_ECOLI | MNTYSITLPWPPSNNRYYRHNRGRTHVSAEGQAYRDNVARIIKNAMLDIGLAMPVKIRIECHMPDRRRRDLDNLQKAAFDALTKAGFWLDDAQVVDYRVVKMPVTKGGRLELTITEMGNE | 3.1.21.10 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000305}; | DNA recombination [GO:0006310]; DNA repair [GO:0006281] | null | crossover junction DNA endonuclease activity [GO:0008821]; four-way junction DNA binding [GO:0000400]; magnesium ion binding [GO:0000287]; protein homodimerization activity [GO:0042803] | PF05866; | 3.30.1330.70; | RusA family | null | null | CATALYTIC ACTIVITY: Reaction=Endonucleolytic cleavage at a junction such as a reciprocal single-stranded crossover between two homologous DNA duplexes (Holliday junction).; EC=3.1.21.10; | null | null | null | null | FUNCTION: Endonuclease that resolves Holliday junction intermediates made during homologous genetic recombination and DNA repair. Exhibits sequence and structure-selective cleavage of four-way DNA junctions, where it introduces symmetrical nicks in two strands of the same polarity at the 5' side of CC dinucleotides. Co... | Escherichia coli (strain K12) |
P0AG80 | UGPB_ECOLI | MKPLHYTASALALGLALMGNAQAVTTIPFWHSMEGELGKEVDSLAQRFNAENPDYKIVPTYKGNYEQNLSAGIAAFRTGNAPAILQVYEVGTATMMASKAIKPVYDVFKEAGIQFDESQFVPTVSGYYSDSKTGHLLSQPFNSSTPVLYYNKDAFKKAGLDPEQPPKTWQDLADYAAKLKASGMKCGYASGWQGWIQLENFSAWNGLPFASKNNGFDGTDAVLEFNKPEQVKHIAMLEEMNKKGDFSYVGRKDESTEKFYNGDCAMTTASSGSLANIREYAKFNYGVGMMPYDADAKDAPQNAIIGGASLWVMQGKDKET... | null | null | glycerol-3-phosphate transmembrane transport [GO:0015794]; glycerophosphodiester transmembrane transport [GO:0001407] | glycerol-3-phosphate-transporting ATPase complex [GO:1902517]; membrane [GO:0016020]; outer membrane-bounded periplasmic space [GO:0030288] | null | PF13416; | 3.40.190.10; | Bacterial solute-binding protein 1 family | null | SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:32882062}. | null | null | null | null | null | FUNCTION: Part of the ABC transporter complex UgpBAEC involved in sn-glycerol-3-phosphate (G3P) import (PubMed:23013274, PubMed:2842304). Can also transport glycerophosphoryl diesters, which are hydrolyzed to G3P and alcohol during transport (PubMed:2842304). The G3P moiety can be detected in the cytoplasm whereas the ... | Escherichia coli (strain K12) |
P0AG86 | SECB_ECOLI | MSEQNNTEMTFQIQRIYTKDISFEAPNAPHVFQKDWQPEVKLDLDTASSQLADDVYEVVLRVTVTASLGEETAFLCEVQQGGIFSIAGIEGTQMAHCLGAYCPNILFPYARECITSMVSRGTFPQLNLAPVNFDALFMNYLQQQAGEGTEEHQDA | null | null | localization [GO:0051179]; maintenance of unfolded protein [GO:0036506]; protein folding [GO:0006457]; protein localization [GO:0008104]; protein targeting [GO:0006605]; protein tetramerization [GO:0051262]; protein transport [GO:0015031]; protein transport by the Sec complex [GO:0043952] | cytosol [GO:0005829] | preprotein binding [GO:0070678]; unfolded protein binding [GO:0051082] | PF02556; | 3.10.420.10; | SecB family | null | SUBCELLULAR LOCATION: Cytoplasm. | null | null | null | null | null | FUNCTION: One of the proteins required for the normal export of some preproteins out of the cell cytoplasm. It is a molecular chaperone that binds to a subset of precursor proteins, maintaining them in a translocation-competent state. For 2 proteins (MBP, MalE and PhoA) the substrate is wrapped around the homotetramer,... | Escherichia coli (strain K12) |
P0AG90 | SECD_ECOLI | MLNRYPLWKYVMLIVVIVIGLLYALPNLFGEDPAVQITGARGVAASEQTLIQVQKTLQEEKITAKSVALEEGAILARFDSTDTQLRAREALMGVMGDKYVVALNLAPATPRWLAAIHAEPMKLGLDLRGGVHFLMEVDMDTALGKLQEQNIDSLRSDLREKGIPYTTVRKENNYGLSITFRDAKARDEAIAYLSKRHPDLVISSQGSNQLRAVMSDARLSEAREYAVQQNINILRNRVNQLGVAEPVVQRQGADRIVVELPGIQDTARAKEILGATATLEFRLVNTNVDQAAAASGRVPGDSEVKQTREGQPVVLYKRVI... | null | null | intracellular protein transmembrane transport [GO:0065002]; protein insertion into membrane from inner side [GO:0032978]; protein targeting [GO:0006605]; protein transport [GO:0015031]; protein transport by the Sec complex [GO:0043952] | cell envelope Sec protein transport complex [GO:0031522]; membrane [GO:0016020]; plasma membrane [GO:0005886] | protein-transporting ATPase activity [GO:0015450] | PF07549;PF13721;PF21760;PF02355; | 3.30.1360.200;3.30.70.260;3.30.70.3400;1.20.1640.10; | SecD/SecF family, SecD subfamily | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:16079137}; Multi-pass membrane protein {ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:16079137}. | null | null | null | null | null | FUNCTION: Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA. The large periplasmic domain is thought to have a base and head domain joined by a hinge; m... | Escherichia coli (strain K12) |
P0AG93 | SECF_ECOLI | MAQEYTVEQLNHGRKVYDFMRWDYWAFGISGLLLIAAIVIMGVRGFNWGLDFTGGTVIEITLEKPAEIDVMRDALQKAGFEEPMLQNFGSSHDIMVRMPPAEGETGGQVLGSQVLKVINESTNQNAAVKRIEFVGPSVGADLAQTGAMALMAALLSILVYVGFRFEWRLAAGVVIALAHDVIITLGILSLFHIEIDLTIVASLMSVIGYSLNDSIVVSDRIRENFRKIRRGTPYEIFNVSLTQTLHRTLITSGTTLMVILMLYLFGGPVLEGFSLTMLIGVSIGTASSIYVASALALKLGMKREHMLQQKVEKEGADQPS... | null | null | intracellular protein transmembrane transport [GO:0065002]; protein insertion into membrane from inner side [GO:0032978]; protein targeting [GO:0006605]; protein transport [GO:0015031]; protein transport by the Sec complex [GO:0043952] | cell envelope Sec protein transport complex [GO:0031522]; membrane [GO:0016020]; plasma membrane [GO:0005886] | protein-transporting ATPase activity [GO:0015450] | PF07549;PF02355; | 1.20.1640.10; | SecD/SecF family, SecF subfamily | null | SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. | null | null | null | null | null | FUNCTION: Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA. The large periplasmic domain is thought to have a base and head domain joined by a hinge; m... | Escherichia coli (strain K12) |
P0AG96 | SECE_ECOLI | MSANTEAQGSGRGLEAMKWVVVVALLLVAIVGNYLYRDIMLPLRALAVVILIAAAGGVALLTTKGKATVAFAREARTEVRKVIWPTRQETLHTTLIVAAVTAVMSLILWGLDGILVRLVSFITGLRF | null | null | intracellular protein transmembrane transport [GO:0065002]; intracellular protein transport [GO:0006886]; protein insertion into membrane from inner side [GO:0032978]; protein secretion [GO:0009306]; protein transport by the Sec complex [GO:0043952]; SRP-dependent cotranslational protein targeting to membrane, transloc... | cell envelope Sec protein transport complex [GO:0031522]; membrane [GO:0016020]; plasma membrane [GO:0005886] | protein transmembrane transporter activity [GO:0008320] | PF00584; | 1.20.5.1030; | SecE/SEC61-gamma family | PTM: Degraded by FtsH when the SecYEG complex is jammed or upon treatment with antibiotics that block translation elongation such as chloramphenicol. | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_00422, ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00422, ECO:0000269|PubMed:15919996}. | null | null | null | null | null | FUNCTION: Essential subunit of the protein translocation channel SecYEG. Clamps together the 2 halves of SecY. May contact the channel plug during translocation. Overexpression of some hybrid proteins has been thought to jam the protein secretion apparatus resulting in cell death; while this may be true it also results... | Escherichia coli (strain K12) |
P0AG99 | SECG_ECOLI | MYEALLVVFLIVAIGLVGLIMLQQGKGADMGASFGAGASATLFGSSGSGNFMTRMTALLATLFFIISLVLGNINSNKTNKGSEWENLSAPAKTEQTQPAAPAKPTSDIPN | null | null | intracellular protein transmembrane transport [GO:0065002]; intracellular protein transport [GO:0006886]; protein insertion into membrane from inner side [GO:0032978]; protein secretion [GO:0009306]; protein transport by the Sec complex [GO:0043952]; SRP-dependent cotranslational protein targeting to membrane, transloc... | cell envelope Sec protein transport complex [GO:0031522]; membrane [GO:0016020]; plasma membrane [GO:0005886] | protein transmembrane transporter activity [GO:0008320]; protein-transporting ATPase activity [GO:0015450] | PF03840; | null | SecG family | PTM: The N-terminus is blocked. | SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. | null | null | null | null | null | FUNCTION: Subunit of the protein translocation channel SecYEG. Overexpression of some hybrid proteins has been thought to jam the protein secretion apparatus resulting in cell death; while this may be true it also results in FtsH-mediated degradation of SecY. Treatment with antibiotics that block translation elongation... | Escherichia coli (strain K12) |
P0AGA2 | SECY_ECOLI | MAKQPGLDFQSAKGGLGELKRRLLFVIGALIVFRIGSFIPIPGIDAAVLAKLLEQQRGTIIEMFNMFSGGALSRASIFALGIMPYISASIIIQLLTVVHPTLAEIKKEGESGRRKISQYTRYGTLVLAIFQSIGIATGLPNMPGMQGLVINPGFAFYFTAVVSLVTGTMFLMWLGEQITERGIGNGISIIIFAGIVAGLPPAIAHTIEQARQGDLHFLVLLLVAVLVFAVTFFVVFVERGQRRIVVNYAKRQQGRRVYAAQSTHLPLKVNMAGVIPAIFASSIILFPATIASWFGGGTGWNWLTTISLYLQPGQPLYVLL... | null | null | intracellular protein transmembrane transport [GO:0065002]; intracellular protein transport [GO:0006886]; protein insertion into membrane from inner side [GO:0032978]; protein transport by the Sec complex [GO:0043952]; SRP-dependent cotranslational protein targeting to membrane, translocation [GO:0006616] | cell envelope Sec protein transport complex [GO:0031522]; membrane [GO:0016020]; plasma membrane [GO:0005886] | protein transmembrane transporter activity [GO:0008320]; signal sequence binding [GO:0005048] | PF00344; | 1.10.3370.10; | SecY/SEC61-alpha family | PTM: SecY that is not part of the protein translocation apparatus is degraded by FtsH. Also degraded by FtsH when the SecYEG complex is jammed, or upon treatment with antibiotics that block translation elongation such as chloramphenicol. | SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. | null | null | null | null | null | FUNCTION: The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring compos... | Escherichia coli (strain K12) |
P0AGB0 | SERB_ECOLI | MPNITWCDLPEDVSLWPGLPLSLSGDEVMPLDYHAGRSGWLLYGRGLDKQRLTQYQSKLGAAMVIVAAWCVEDYQVIRLAGSLTARATRLAHEAQLDVAPLGKIPHLRTPGLLVMDMDSTAIQIECIDEIAKLAGTGEMVAEVTERAMRGELDFTASLRSRVATLKGADANILQQVRENLPLMPGLTQLVLKLETLGWKVAIASGGFTFFAEYLRDKLRLTAVVANELEIMDGKFTGNVIGDIVDAQYKAKTLTRLAQEYEIPLAQTVAIGDGANDLPMIKAAGLGIAYHAKPKVNEKAEVTIRHADLMGVFCILSGSLN... | 3.1.3.3 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:16990279}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:16990279}; Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000269|PubMed:16990279}; Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:16990279}; No... | amino acid biosynthetic process [GO:0008652]; dephosphorylation [GO:0016311]; L-serine biosynthetic process [GO:0006564] | cytoplasm [GO:0005737] | L-phosphoserine phosphatase activity [GO:0036424]; magnesium ion binding [GO:0000287]; phosphatase activity [GO:0016791] | PF18429;PF12710; | 3.30.70.2020;3.40.50.1000; | HAD-like hydrolase superfamily, SerB family | null | null | CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-serine = L-serine + phosphate; Xref=Rhea:RHEA:21208, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384, ChEBI:CHEBI:43474, ChEBI:CHEBI:57524; EC=3.1.3.3; CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-D-serine = D-serine + phosphate; Xref=Rhea:RHEA:24873, ChEBI:CHEBI:15377, ChEBI:CHEBI:3... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.097 mM for P-Ser (with magnesium ions as cofactor and at pH 9) {ECO:0000269|PubMed:16990279}; KM=0.07 mM for imido-diphosphate (with magnesium ions as cofactor and at pH 9) {ECO:0000269|PubMed:16990279}; KM=6.2 mM for acetyl-phosphate (with magnesium ions as cofa... | PATHWAY: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from 3-phospho-D-glycerate: step 3/3. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is between 6 and 7.5. {ECO:0000269|PubMed:16990279}; | null | FUNCTION: Catalyzes the dephosphorylation of phosphoserine (P-Ser). Also catalyzes the hydrolysis of phosphothreonine (P-Thr). {ECO:0000269|PubMed:16990279}. | Escherichia coli (strain K12) |
P0AGB3 | RPOH_ECOLI | MTDKMQSLALAPVGNLDSYIRAANAWPMLSADEERALAEKLHYHGDLEAAKTLILSHLRFVVHIARNYAGYGLPQADLIQEGNIGLMKAVRRFNPEVGVRLVSFAVHWIKAEIHEYVLRNWRIVKVATTKAQRKLFFNLRKTKQRLGWFNQDEVEMVARELGVTSKDVREMESRMAAQDMTFDLSSDDDSDSQPMAPVLYLQDKSSNFADGIEDDNWEEQAANRLTDAMQGLDERSQDIIRARWLDEDNKSTLQELADRYGVSAERVRQLEKNAMKKLRAAIEA | null | null | DNA recombination [GO:0006310]; DNA-templated transcription [GO:0006351]; DNA-templated transcription initiation [GO:0006352]; regulation of DNA-templated transcription [GO:0006355]; regulation of DNA-templated transcription initiation [GO:2000142]; regulation of gene expression [GO:0010468]; response to heat [GO:00094... | cytosol [GO:0005829]; cytosolic DNA-directed RNA polymerase complex [GO:0000345]; invertasome [GO:0031421]; plasma membrane [GO:0005886] | bacterial-type RNA polymerase core enzyme binding [GO:0001000]; core promoter sequence-specific DNA binding [GO:0001046]; DNA binding [GO:0003677]; DNA-binding transcription activator activity [GO:0001216]; sigma factor activity [GO:0016987]; site-specific recombinase activity [GO:0009009] | PF04542;PF04545; | 1.20.120.1810;1.20.140.160; | Sigma-70 factor family, RpoH subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00961}. | null | null | null | null | null | FUNCTION: Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor is involved in regulation of expression of heat shock genes. Intracellular concentration of free RpoH protein increases in response to heat shock, which caus... | Escherichia coli (strain K12) |
P0AGB6 | RPOE_ECOLI | MSEQLTDQVLVERVQKGDQKAFNLLVVRYQHKVASLVSRYVPSGDVPDVVQEAFIKAYRALDSFRGDSAFYTWLYRIAVNTAKNYLVAQGRRPPSSDVDAIEAENFESGGALKEISNPENLMLSEELRQIVFRTIESLPEDLRMAITLRELDGLSYEEIAAIMDCPVGTVRSRIFRAREAIDNKVQPLIRR | null | null | cellular response to cell envelope stress [GO:0036460]; DNA-templated transcription initiation [GO:0006352]; negative regulation of DNA-templated transcription [GO:0045892]; regulation of DNA-templated transcription [GO:0006355]; regulation of DNA-templated transcription initiation [GO:2000142]; response to osmotic str... | cytoplasm [GO:0005737]; cytosolic DNA-directed RNA polymerase complex [GO:0000345]; plasma membrane [GO:0005886]; sigma factor antagonist complex [GO:1903865] | DNA binding [GO:0003677]; sigma factor activity [GO:0016987] | PF04542;PF08281; | 1.10.1740.10;1.10.10.10; | Sigma-70 factor family, ECF subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11777003, ECO:0000269|PubMed:9159522}. Note=Associates with the inner membrane via RseA (PubMed:11777003, PubMed:9159522). {ECO:0000269|PubMed:11777003}. | null | null | null | null | null | FUNCTION: Sigma factors are initiation factors that promote the attachment of RNA polymerase (RNAP) to specific initiation sites and are then released (PubMed:2691330, PubMed:7889935, PubMed:9159522, PubMed:9159523). Extracytoplasmic function (ECF) sigma-E controls the envelope stress response, responding to periplasmi... | Escherichia coli (strain K12) |
P0AGC0 | UHPT_ECOLI | MLAFLNQVRKPTLDLPLEVRRKMWFKPFMQSYLVVFIGYLTMYLIRKNFNIAQNDMISTYGLSMTQLGMIGLGFSITYGVGKTLVSYYADGKNTKQFLPFMLILSAICMLGFSASMGSGSVSLFLMIAFYALSGFFQSTGGSCSYSTITKWTPRRKRGTFLGFWNISHNLGGAGAAGVALFGANYLFDGHVIGMFIFPSIIALIVGFIGLRYGSDSPESYGLGKAEELFGEEISEEDKETESTDMTKWQIFVEYVLKNKVIWLLCFANIFLYVVRIGIDQWSTVYAFQELKLSKAVAIQGFTLFEAGALVGTLLWGWLSD... | null | null | glucose-6-phosphate transport [GO:0015760]; hexose phosphate transport [GO:0015712]; phosphate ion transmembrane transport [GO:0035435] | plasma membrane [GO:0005886] | glucose 6-phosphate:inorganic phosphate antiporter activity [GO:0061513]; hexose-phosphate:inorganic phosphate antiporter activity [GO:0015526] | PF07690; | 1.20.1250.20; | Major facilitator superfamily, Organophosphate:Pi antiporter (OPA) (TC 2.A.1.4) family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:2156798, ECO:0000269|PubMed:8402899}; Multi-pass membrane protein {ECO:0000255, ECO:0000269|PubMed:2156798}. | null | null | null | null | null | FUNCTION: Mediates the exchange of external hexose 6-phosphate and internal inorganic phosphate. Can transport glucose-6-phosphate, fructose-6-phosphate and mannose-6-phosphate. Also catalyzes the neutral exchange of internal and external phosphate. {ECO:0000269|PubMed:2197272, ECO:0000269|PubMed:3038843, ECO:0000269|P... | Escherichia coli (strain K12) |
P0AGC3 | SLT_ECOLI | MEKAKQVTWRLLAAGVCLLTVSSVARADSLDEQRSRYAQIKQAWDNRQMDVVEQMMPGLKDYPLYPYLEYRQITDDLMNQPAVTVTNFVRANPTLPPARTLQSRFVNELARREDWRGLLAFSPEKPGTTEAQCNYYYAKWNTGQSEEAWQGAKELWLTGKSQPNACDKLFSVWRASGKQDPLAYLERIRLAMKAGNTGLVTVLAGQMPADYQTIASAIISLANNPNTVLTFARTTGATDFTRQMAAVAFASVARQDAENARLMIPSLAQAQQLNEDQIQELRDIVAWRLMGNDVTDEQAKWRDDAIMRSQSTSLIERRVR... | 4.2.2.n1 | null | cell wall organization [GO:0071555]; peptidoglycan catabolic process [GO:0009253] | membrane [GO:0016020]; outer membrane-bounded periplasmic space [GO:0030288]; peptidoglycan-based cell wall [GO:0009274] | hydrolase activity, hydrolyzing O-glycosyl compounds [GO:0004553]; lytic endotransglycosylase activity [GO:0008932]; lytic transglycosylase activity [GO:0008933] | PF01464;PF14718; | 1.10.530.10;1.25.20.10;1.10.1240.20; | Transglycosylase Slt family | null | SUBCELLULAR LOCATION: Periplasm. Note=Tightly associated with the murein sacculus. | CATALYTIC ACTIVITY: Reaction=Exolytic cleavage of the (1->4)-beta-glycosidic linkage between N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (GlcNAc) residues in peptidoglycan, from either the reducing or the non-reducing ends of the peptidoglycan chains, with concomitant formation of a 1,6-anhydrobond in the Mur... | null | null | null | null | FUNCTION: Murein-degrading enzyme. Catalyzes the cleavage of the glycosidic bonds between N-acetylmuramic acid and N-acetylglucosamine residues in peptidoglycan. May play a role in recycling of muropeptides during cell elongation and/or cell division. | Escherichia coli (strain K12) |
P0AGD1 | SODC_ECOLI | MKRFSLAILALVVATGAQAASEKVEMNLVTSQGVGQSIGSVTITETDKGLEFSPDLKALPPGEHGFHIHAKGSCQPATKDGKASAAESAGGHLDPQNTGKHEGPEGAGHLGDLPALVVNNDGKATDAVIAPRLKSLDEIKDKALMVHVGGDNMSDQPKPLGGGGERYACGVIK | 1.15.1.1 | COFACTOR: Name=Cu cation; Xref=ChEBI:CHEBI:23378; Note=Binds 1 copper ion per subunit.; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 1 zinc ion per subunit.; | removal of superoxide radicals [GO:0019430]; superoxide metabolic process [GO:0006801] | outer membrane-bounded periplasmic space [GO:0030288]; periplasmic space [GO:0042597] | copper ion binding [GO:0005507]; superoxide dismutase activity [GO:0004784]; zinc ion binding [GO:0008270] | PF00080; | 2.60.40.200; | Cu-Zn superoxide dismutase family | null | SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:7589534, ECO:0000269|PubMed:7786035}. | CATALYTIC ACTIVITY: Reaction=2 H(+) + 2 superoxide = H2O2 + O2; Xref=Rhea:RHEA:20696, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:18421; EC=1.15.1.1; Evidence={ECO:0000269|PubMed:7929223, ECO:0000269|PubMed:8626323}; | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.8. {ECO:0000269|PubMed:7929223}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Highly thermostable.; | FUNCTION: Destroys radicals which are normally produced within the cells and which are toxic to biological systems. | Escherichia coli (strain K12) |
P0AGD3 | SODF_ECOLI | MSFELPALPYAKDALAPHISAETIEYHYGKHHQTYVTNLNNLIKGTAFEGKSLEEIIRSSEGGVFNNAAQVWNHTFYWNCLAPNAGGEPTGKVAEAIAASFGSFADFKAQFTDAAIKNFGSGWTWLVKNSDGKLAIVSTSNAGTPLTTDATPLLTVDVWEHAYYIDYRNARPGYLEHFWALVNWEFVAKNLAA | 1.15.1.1 | COFACTOR: Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000269|PubMed:9125513}; Note=Binds 1 Fe cation per subunit. {ECO:0000269|PubMed:9125513}; | removal of superoxide radicals [GO:0019430]; response to superoxide [GO:0000303]; superoxide metabolic process [GO:0006801] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; membrane [GO:0016020] | iron ion binding [GO:0005506]; oxidoreductase activity [GO:0016491]; superoxide dismutase activity [GO:0004784] | PF02777;PF00081; | 1.10.287.990;3.55.40.20; | Iron/manganese superoxide dismutase family | null | null | CATALYTIC ACTIVITY: Reaction=2 H(+) + 2 superoxide = H2O2 + O2; Xref=Rhea:RHEA:20696, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:18421; EC=1.15.1.1; Evidence={ECO:0000269|PubMed:9125513}; | null | null | null | null | FUNCTION: Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems. | Escherichia coli (strain K12) |
P0AGD7 | SRP54_ECOLI | MFDNLTDRLSRTLRNISGRGRLTEDNVKDTLREVRMALLEADVALPVVREFINRVKEKAVGHEVNKSLTPGQEFVKIVRNELVAAMGEENQTLNLAAQPPAVVLMAGLQGAGKTTSVGKLGKFLREKHKKKVLVVSADVYRPAAIKQLETLAEQVGVDFFPSDVGQKPVDIVNAALKEAKLKFYDVLLVDTAGRLHVDEAMMDEIKQVHASINPVETLFVVDAMTGQDAANTAKAFNEALPLTGVVLTKVDGDARGGAALSIRHITGKPIKFLGVGEKTEALEPFHPDRIASRILGMGDVLSLIEDIESKVDRAQAEKLA... | 3.6.5.4 | null | protein targeting to membrane [GO:0006612]; SRP-dependent cotranslational protein targeting to membrane, translocation [GO:0006616] | cytosol [GO:0005829]; ribonucleoprotein complex [GO:1990904]; signal recognition particle [GO:0048500] | 7S RNA binding [GO:0008312]; ATP hydrolysis activity [GO:0016887]; endoplasmic reticulum signal peptide binding [GO:0030942]; GTP binding [GO:0005525]; GTPase activity [GO:0003924] | PF00448;PF02881;PF02978; | 3.40.50.300;1.20.120.140;1.10.260.30; | GTP-binding SRP family, SRP54 subfamily | null | SUBCELLULAR LOCATION: Cytoplasm. Note=The SRP-RNC complex is targeted to the cytoplasmic membrane. | CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00306, ECO:0000269|PubMed:11735405}; | null | null | null | null | FUNCTION: Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Binds to the hydrophobic signal sequence of the ribosome-nascent chain (RNC) as it emerges from the ribosomes. The SRP-RNC complex is then targeted to the cytoplasmic membrane where it interacts with the SRP recept... | Escherichia coli (strain K12) |
P0AGE0 | SSB_ECOLI | MASRGVNKVILVGNLGQDPEVRYMPNGGAVANITLATSESWRDKATGEMKEQTEWHRVVLFGKLAEVASEYLRKGSQVYIEGQLRTRKWTDQSGQDRYTTEVVVNVGGTMQMLGGRQGGGAPAGGNIGGGQPQGGWGQPQQPQGGNQFSGGAQSRPQQSAPAAPSNEPPMDFDDDIPF | null | null | DNA-templated DNA replication [GO:0006261]; mismatch repair [GO:0006298]; positive regulation of catalytic activity [GO:0043085]; recombinational repair [GO:0000725]; SOS response [GO:0009432] | cytosol [GO:0005829]; nucleoid [GO:0009295]; replisome [GO:0030894]; single-stranded DNA-binding protein complex [GO:0044777] | enzyme activator activity [GO:0008047]; identical protein binding [GO:0042802]; single-stranded DNA binding [GO:0003697] | PF00436; | 2.40.50.140; | null | PTM: Phosphorylated on tyrosine residue(s). {ECO:0000269|PubMed:16549871}. | null | null | null | null | null | null | FUNCTION: Plays an important role in DNA replication, recombination and repair. Binds to ssDNA and to an array of partner proteins to recruit them to their sites of action during DNA metabolism. Acts as a sliding platform that migrates on DNA via reptation. SSB or its 10 C-terminal amino acids stimulates the ATPase act... | Escherichia coli (strain K12) |
P0AGE4 | SSTT_ECOLI | MTTQRSPGLFRRLAHGSLVKQILVGLVLGILLAWISKPAAEAVGLLGTLFVGALKAVAPILVLMLVMASIANHQHGQKTNIRPILFLYLLGTFSAALAAVVFSFAFPSTLHLSSSAGDISPPSGIVEVMRGLVMSMVSNPIDALLKGNYIGILVWAIGLGFALRHGNETTKNLVNDMSNAVTFMVKLVIRFAPIGIFGLVSSTLATTGFSTLWGYAQLLVVLVGCMLLVALVVNPLLVWWKIRRNPFPLVLLCLRESGVYAFFTRSSAANIPVNMALCEKLNLDRDTYSVSIPLGATINMAGAAITITVLTLAAVNTLGI... | null | null | amino acid transport [GO:0006865]; serine transport [GO:0032329]; threonine transport [GO:0015826] | plasma membrane [GO:0005886] | neutral L-amino acid transmembrane transporter activity [GO:0015175]; neutral L-amino acid:sodium symporter activity [GO:0005295] | PF00375; | 1.10.3860.10; | Dicarboxylate/amino acid:cation symporter (DAACS) (TC 2.A.23) family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_01582, ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01582}. | CATALYTIC ACTIVITY: Reaction=L-serine(in) + Na(+)(in) = L-serine(out) + Na(+)(out); Xref=Rhea:RHEA:29575, ChEBI:CHEBI:29101, ChEBI:CHEBI:33384; Evidence={ECO:0000255|HAMAP-Rule:MF_01582, ECO:0000269|PubMed:12097162, ECO:0000269|PubMed:9852024}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:29577; Evidence={ECO:0... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.82 uM for serine {ECO:0000269|PubMed:12097162}; Vmax=0.37 umol/min/mg enzyme {ECO:0000269|PubMed:12097162}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0. {ECO:0000269|PubMed:12097162}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 40 degrees Celsius. {ECO:0000269|PubMed:12097162}; | FUNCTION: Involved in the import of serine and threonine into the cell, with the concomitant import of sodium (symport system). {ECO:0000255|HAMAP-Rule:MF_01582, ECO:0000269|PubMed:12097162, ECO:0000269|PubMed:9852024}. | Escherichia coli (strain K12) |
P0AGE6 | CHRR_ECOLI | MSEKLQVVTLLGSLRKGSFNGMVARTLPKIAPASMEVNALPSIADIPLYDADVQQEEGFPATVEALAEQIRQADGVVIVTPEYNYSVPGGLKNAIDWLSRLPDQPLAGKPVLIQTSSMGVIGGARCQYHLRQILVFLDAMVMNKPEFMGGVIQNKVDPQTGEVIDQGTLDHLTGQLTAFGEFIQRVKI | 1.6.-.-; 1.6.5.2 | COFACTOR: Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000269|PubMed:14766567, ECO:0000269|PubMed:22558308}; Note=Binds 1 FMN per subunit. {ECO:0000269|PubMed:22558308}; | protein homotetramerization [GO:0051289]; xenobiotic metabolic process [GO:0006805] | cytosol [GO:0005829] | chromate reductase activity [GO:0034567]; FMN binding [GO:0010181]; identical protein binding [GO:0042802]; NADH dehydrogenase (quinone) activity [GO:0050136]; NADPH dehydrogenase (quinone) activity [GO:0008753]; oxidoreductase activity [GO:0016491] | PF03358; | 3.40.50.360; | SsuE family | null | null | CATALYTIC ACTIVITY: Reaction=a quinone + H(+) + NADH = a quinol + NAD(+); Xref=Rhea:RHEA:46160, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:132124; EC=1.6.5.2; Evidence={ECO:0000269|PubMed:14766567}; CATALYTIC ACTIVITY: Reaction=a quinone + H(+) + NADPH = a quinol + NADP(+); ... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=108 uM for uranyl (at pH 7 and 37 degrees Celsius) {ECO:0000269|PubMed:17088379}; KM=200 uM for chromate (at pH 5 and 35 degrees Celsius) {ECO:0000269|PubMed:14766567}; KM=376 uM for chromate (at pH 7 and 37 degrees Celsius) {ECO:0000269|PubMed:17088379}; Vmax=5 um... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5. {ECO:0000269|PubMed:14766567}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 35 degrees Celsius. {ECO:0000269|PubMed:14766567}; | FUNCTION: Catalyzes the reduction of quinones (PubMed:14766567). Acts by simultaneous two-electron transfer, avoiding formation of highly reactive semiquinone intermediates and producing quinols that promote tolerance of H(2)O(2). Quinone reduction is probably the primary biological role of ChrR (By similarity). Can al... | Escherichia coli (strain K12) |
P0AGE9 | SUCD_ECOLI | MSILIDKNTKVICQGFTGSQGTFHSEQAIAYGTKMVGGVTPGKGGTTHLGLPVFNTVREAVAATGATASVIYVPAPFCKDSILEAIDAGIKLIITITEGIPTLDMLTVKVKLDEAGVRMIGPNCPGVITPGECKIGIQPGHIHKPGKVGIVSRSGTLTYEAVKQTTDYGFGQSTCVGIGGDPIPGSNFIDILEMFEKDPQTEAIVMIGEIGGSAEEEAAAYIKEHVTKPVVGYIAGVTAPKGKRMGHAGAIIAGGKGTADEKFAALEAAGVKTVRSLADIGEALKTVLK | 6.2.1.5 | null | tricarboxylic acid cycle [GO:0006099] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; succinate-CoA ligase complex (ADP-forming) [GO:0009361] | nucleotide binding [GO:0000166]; succinate-CoA ligase (ADP-forming) activity [GO:0004775]; succinate-CoA ligase (GDP-forming) activity [GO:0004776] | PF02629;PF00549; | 3.40.50.720;3.40.50.261; | Succinate/malate CoA ligase alpha subunit family | null | null | CATALYTIC ACTIVITY: Reaction=ATP + CoA + succinate = ADP + phosphate + succinyl-CoA; Xref=Rhea:RHEA:17661, ChEBI:CHEBI:30031, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292, ChEBI:CHEBI:456216; EC=6.2.1.5; Evidence={ECO:0000255|HAMAP-Rule:MF_01988, ECO:0000269|PubMed:10353839}; Physiological... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.25 mM for succinate {ECO:0000269|PubMed:10353839}; KM=4 uM for CoA {ECO:0000269|PubMed:10353839}; Note=kcat is 2684 min(-1) with ATP as substrate and 1471 min(-1) with GTP as substrate. {ECO:0000269|PubMed:10353839}; | PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; succinate from succinyl-CoA (ligase route): step 1/1. {ECO:0000255|HAMAP-Rule:MF_01988, ECO:0000305|PubMed:10353839}. | null | null | FUNCTION: Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The alpha subunit of the enzyme binds the substrates coenzyme A and phosphate, while ... | Escherichia coli (strain K12) |
P0AGF2 | CSDE_ECOLI | MTNPQFAGHPFGTTVTAETLRNTFAPLTQWEDKYRQLIMLGKQLPALPDELKAQAKEIAGCENRVWLGYTVAENGKMHFFGDSEGRIVRGLLAVLLTAVEGKTAAELQAQSPLALFDELGLRAQLSASRSQGLNALSEAIIAATKQV | null | null | cyclic threonylcarbamoyladenosine biosynthetic process [GO:0061504] | null | sulfur carrier activity [GO:0097163] | PF02657; | 3.90.1010.10; | SufE family | null | null | null | null | null | null | null | FUNCTION: Stimulates the cysteine desulfurase activity of CsdA. Contains a cysteine residue (Cys-61) that acts to accept sulfur liberated via the desulfurase activity of CsdA. May be able to transfer sulfur to TcdA/CsdL. Seems to support the function of TcdA in the generation of cyclic threonylcarbamoyladenosine at pos... | Escherichia coli (strain K12) |
P0AGF4 | XYLE_ECOLI | MNTQYNSSYIFSITLVATLGGLLFGYDTAVISGTVESLNTVFVAPQNLSESAANSLLGFCVASALIGCIIGGALGGYCSNRFGRRDSLKIAAVLFFISGVGSAWPELGFTSINPDNTVPVYLAGYVPEFVIYRIIGGIGVGLASMLSPMYIAELAPAHIRGKLVSFNQFAIIFGQLLVYCVNYFIARSGDASWLNTDGWRYMFASECIPALLFLMLLYTVPESPRWLMSRGKQEQAEGILRKIMGNTLATQAVQEIKHSLDHGRKTGGRLLMFGVGVIVIGVMLSIFQQFVGINVVLYYAPEVFKTLGASTDIALLQTII... | null | null | D-xylose transmembrane transport [GO:0015753]; transmembrane transport [GO:0055085] | membrane [GO:0016020]; plasma membrane [GO:0005886] | D-xylose:proton symporter activity [GO:0015519]; glucose transmembrane transporter activity [GO:0005355]; transmembrane transporter activity [GO:0022857] | PF00083; | 1.20.1250.20; | Major facilitator superfamily, Sugar transporter (TC 2.A.1.1) family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:23075985}; Multi-pass membrane protein {ECO:0000269|PubMed:23075985}. | CATALYTIC ACTIVITY: Reaction=D-xylose(in) + H(+)(in) = D-xylose(out) + H(+)(out); Xref=Rhea:RHEA:28959, ChEBI:CHEBI:15378, ChEBI:CHEBI:53455; Evidence={ECO:0000269|PubMed:23075985}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:28961; Evidence={ECO:0000269|PubMed:23075985}; | null | null | null | null | FUNCTION: Uptake of D-xylose across the boundary membrane with the concomitant transport of protons into the cell (symport system). Glucose is not transported, but can compete for xylose binding sites and can inhibit xylose transport (in vitro). {ECO:0000269|PubMed:23075985}. | Escherichia coli (strain K12) |
P0AGF6 | TDCB_ECOLI | MHITYDLPVAIDDIIEAKQRLAGRIYKTGMPRSNYFSERCKGEIFLKFENMQRTGSFKIRGAFNKLSSLTDAEKRKGVVACSAGNHAQGVSLSCAMLGIDGKVVMPKGAPKSKVAATCDYSAEVVLHGDNFNDTIAKVSEIVEMEGRIFIPPYDDPKVIAGQGTIGLEIMEDLYDVDNVIVPIGGGGLIAGIAVAIKSINPTIRVIGVQSENVHGMAASFHSGEITTHRTTGTLADGCDVSRPGNLTYEIVRELVDDIVLVSEDEIRNSMIALIQRNKVVTEGAGALACAALLSGKLDQYIQNRKTVSIISGGNIDLSRV... | 4.3.1.17; 4.3.1.19 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000269|PubMed:5321308}; | isoleucine biosynthetic process [GO:0009097]; L-serine catabolic process [GO:0006565]; L-threonine catabolic process to propionate [GO:0070689]; threonine catabolic process [GO:0006567] | cytosol [GO:0005829]; protein-containing complex [GO:0032991] | amino acid binding [GO:0016597]; L-serine ammonia-lyase activity [GO:0003941]; nucleotide binding [GO:0000166]; pyridoxal phosphate binding [GO:0030170]; threonine aldolase activity [GO:0004793]; threonine deaminase activity [GO:0004794] | PF00291; | 3.40.50.1100; | Serine/threonine dehydratase family | null | null | CATALYTIC ACTIVITY: Reaction=L-threonine = 2-oxobutanoate + NH4(+); Xref=Rhea:RHEA:22108, ChEBI:CHEBI:16763, ChEBI:CHEBI:28938, ChEBI:CHEBI:57926; EC=4.3.1.19; CATALYTIC ACTIVITY: Reaction=L-serine = NH4(+) + pyruvate; Xref=Rhea:RHEA:19169, ChEBI:CHEBI:15361, ChEBI:CHEBI:28938, ChEBI:CHEBI:33384; EC=4.3.1.17; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.3 uM for L-threonine (at 37 dregrees Celsius and at pH 7.8) {ECO:0000269|PubMed:15390404}; KM=0.35 uM for L-serine (at 37 dregrees Celsius and at pH 7.8) {ECO:0000269|PubMed:15390404}; | PATHWAY: Amino-acid degradation; L-threonine degradation via propanoate pathway; propanoate from L-threonine: step 1/4. | null | null | FUNCTION: Catalyzes the anaerobic formation of alpha-ketobutyrate and ammonia from threonine in a two-step reaction. The first step involved a dehydration of threonine and a production of enamine intermediates (aminocrotonate), which tautomerizes to its imine form (iminobutyrate). Both intermediates are unstable and sh... | Escherichia coli (strain K12) |
P0AGG0 | THIL_ECOLI | MACGEFSLIARYFDRVRSSRLDVELGIGDDCALLNIPEKQTLAISTDTLVAGNHFLPDIDPADLAYKALAVNLSDLAAMGADPAWLTLALTLPDVDEAWLESFSDSLFDLLNYYDMQLIGGDTTRGPLSMTLGIHGFVPMGRALTRSGAKPGDWIYVTGTPGDSAAGLAILQNRLQVADAKDADYLIKRHLRPSPRILQGQALRDLANSAIDLSDGLISDLGHIVKASDCGARIDLALLPFSDALSRHVEPEQALRWALSGGEDYELCFTVPELNRGALDVALGHLGVPFTCIGQMTADIEGLCFIRDGEPVTLDWKGYD... | 2.7.4.16 | null | phosphorylation [GO:0016310]; thiamine biosynthetic process [GO:0009228]; thiamine diphosphate biosynthetic process [GO:0009229] | null | ATP binding [GO:0005524]; magnesium ion binding [GO:0000287]; metal ion binding [GO:0046872]; thiamine-phosphate kinase activity [GO:0009030] | PF00586;PF02769; | 3.90.650.10;3.30.1330.10; | Thiamine-monophosphate kinase family | null | null | CATALYTIC ACTIVITY: Reaction=ATP + thiamine phosphate = ADP + thiamine diphosphate; Xref=Rhea:RHEA:15913, ChEBI:CHEBI:30616, ChEBI:CHEBI:37575, ChEBI:CHEBI:58937, ChEBI:CHEBI:456216; EC=2.7.4.16; Evidence={ECO:0000269|PubMed:4567662}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.1 uM for thiamine-monophosphate {ECO:0000269|PubMed:4567662}; KM=270 uM for ATP {ECO:0000269|PubMed:4567662}; | PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; thiamine diphosphate from thiamine phosphate: step 1/1. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is about 8.0. {ECO:0000269|PubMed:4567662}; | null | FUNCTION: Catalyzes the ATP-dependent phosphorylation of thiamine-monophosphate (TMP) to form thiamine-pyrophosphate (TPP), the active form of vitamin B1. Cannot use thiamine as substrate. Is highly specific for ATP as phosphate donor. {ECO:0000269|PubMed:4567662, ECO:0000269|PubMed:6284709}. | Escherichia coli (strain K12) |
P0AGG2 | TESB_ECOLI | MSQALKNLLTLLNLEKIEEGLFRGQSEDLGLRQVFGGQVVGQALYAAKETVPEERLVHSFHSYFLRPGDSKKPIIYDVETLRDGNSFSARRVAAIQNGKPIFYMTASFQAPEAGFEHQKTMPSAPAPDGLPSETQIAQSLAHLLPPVLKDKFICDRPLEVRPVEFHNPLKGHVAEPHRQVWIRANGSVPDDLRVHQYLLGYASDLNFLPVALQPHGIGFLEPGIQIATIDHSMWFHRPFNLNEWLLYSVESTSASSARGFVRGEFYTQDGVLVASTVQEGVMRNHN | 3.1.2.20 | null | acyl-CoA metabolic process [GO:0006637]; fatty acid catabolic process [GO:0009062] | cytosol [GO:0005829]; peroxisomal matrix [GO:0005782] | fatty acyl-CoA hydrolase activity [GO:0047617]; identical protein binding [GO:0042802]; protein homodimerization activity [GO:0042803] | PF13622;PF02551; | 2.40.160.210; | C/M/P thioester hydrolase family | null | null | CATALYTIC ACTIVITY: Reaction=a fatty acyl-CoA + H2O = a fatty acid + CoA + H(+); Xref=Rhea:RHEA:16781, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57287, ChEBI:CHEBI:77636; EC=3.1.2.20; Evidence={ECO:0000269|PubMed:10876240, ECO:0000269|PubMed:14707139, ECO:0000269|PubMed:1645722, ECO:0000269|P... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=13 uM for decanoyl-CoA {ECO:0000269|PubMed:10876240}; KM=9 uM for dodecanoyl-CoA {ECO:0000269|PubMed:18702504}; KM=6 uM for 3,5-dodecadienoyl-CoA {ECO:0000269|PubMed:18702504}; KM=13 uM for tetradecanoyl-CoA {ECO:0000269|PubMed:18702504}; KM=7 uM for 3,5-tetradecad... | null | null | null | FUNCTION: Thioesterase that has relatively broad substrate specificity, hydrolyzing primarily medium- and long-chain acyl-CoA substrates to free fatty acids and CoA (PubMed:1645722, PubMed:20547355, PubMed:24271180). Functions in the thioesterase-dependent pathway of beta-oxidation of oleate and conjugated linoleate ((... | Escherichia coli (strain K12) |
P0AGG3 | TESB_ECO57 | MSQALKNLLTLLNLEKIEEGLFRGQSEDLGLRQVFGGQVVGQALYAAKETVPEERLVHSFHSYFLRPGDSKKPIIYDVETLRDGNSFSARRVAAIQNGKPIFYMTASFQAPEAGFEHQKTMPSAPAPDGLPSETQIAQSLAHLLPPVLKDKFICDRPLEVRPVEFHNPLKGHVAEPHRQVWIRANGSVPDDLRVHQYLLGYASDLNFLPVALQPHGIGFLEPGIQIATIDHSMWFHRPFNLNEWLLYSVESTSASSARGFVRGEFYTQDGVLVASTVQEGVMRNHN | 3.1.2.20 | null | acyl-CoA metabolic process [GO:0006637]; fatty acid catabolic process [GO:0009062] | cytosol [GO:0005829]; peroxisomal matrix [GO:0005782] | fatty acyl-CoA hydrolase activity [GO:0047617] | PF13622;PF02551; | 2.40.160.210; | C/M/P thioester hydrolase family | null | null | CATALYTIC ACTIVITY: Reaction=a fatty acyl-CoA + H2O = a fatty acid + CoA + H(+); Xref=Rhea:RHEA:16781, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57287, ChEBI:CHEBI:77636; EC=3.1.2.20; Evidence={ECO:0000250|UniProtKB:P0AGG2}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16782; Evidence... | null | null | null | null | FUNCTION: Thioesterase that has relatively broad substrate specificity, hydrolyzing primarily medium- and long-chain acyl-CoA substrates to free fatty acids and CoA. Functions in the thioesterase-dependent pathway of beta-oxidation of oleate and conjugated linoleate ((9Z,11E)-octadecadienoate or CLA), which provides al... | Escherichia coli O157:H7 |
P0AGI1 | RBSC_ECOLI | MTTQTVSGRRYFTKAWLMEQKSLIALLVLIAIVSTLSPNFFTINNLFNILQQTSVNAIMAVGMTLVILTSGIDLSVGSLLALTGAVAASIVGIEVNALVAVAAALALGAAIGAVTGVIVAKGRVQAFIATLVMMLLLRGVTMVYTNGSPVNTGFTENADLFGWFGIGRPLGVPTPVWIMGIVFLAAWYMLHHTRLGRYIYALGGNEAATRLSGINVNKIKIIVYSLCGLLASLAGIIEVARLSSAQPTAGTGYELDAIAAVVLGGTSLAGGKGRIVGTLIGALILGFLNNGLNLLGVSSYYQMIVKAVVILLAVLVDNKK... | null | null | D-ribose transmembrane transport [GO:0015752] | ATP-binding cassette (ABC) transporter complex [GO:0043190]; ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing [GO:0055052]; membrane [GO:0016020]; plasma membrane [GO:0005886] | D-ribose transmembrane transporter activity [GO:0015591] | PF02653; | null | Binding-protein-dependent transport system permease family, AraH/RbsC subfamily | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:9922273}; Multi-pass membrane protein {ECO:0000305|PubMed:9922273}. | null | null | null | null | null | FUNCTION: Part of the ABC transporter complex RbsABC involved in ribose import. Probably responsible for the translocation of the substrate across the membrane. {ECO:0000269|PubMed:25533465, ECO:0000269|PubMed:6327617}.; FUNCTION: (Microbial infection) Probably transports the toxic C-terminal region of CdiA from D.dada... | Escherichia coli (strain K12) |
P0AGJ7 | TRML_ECOLI | MLNIVLYEPEIPPNTGNIIRLCANTGFRLHIIEPMGFAWDDKRLRRAGLDYHEFTAVTRHHDYRAFLEAENPQRLFALTTKGTPAHSAVSYQDGDYLMFGPETRGLPASILDALPAEQKIRIPMVPDSRSMNLSNAVSVVVYEAWRQLGYPGAVLRD | 2.1.1.207 | null | wobble position cytosine ribose methylation [GO:0002131]; wobble position uridine ribose methylation [GO:0002132] | cytoplasm [GO:0005737] | protein homodimerization activity [GO:0042803]; RNA binding [GO:0003723]; tRNA (5-carboxymethylaminomethyluridine(34)-2'-O)-methyltransferase activity [GO:0141102]; tRNA (cytidine(34)-2'-O)-methyltransferase activity [GO:0141098]; tRNA (uracil-2'-O-)-methyltransferase activity [GO:0052665] | PF00588; | 3.40.1280.10; | Class IV-like SAM-binding methyltransferase superfamily, RNA methyltransferase TrmH family, TrmL subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01885}. | CATALYTIC ACTIVITY: Reaction=cytidine(34) in tRNA + S-adenosyl-L-methionine = 2'-O-methylcytidine(34) in tRNA + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:43084, Rhea:RHEA-COMP:10331, Rhea:RHEA-COMP:10332, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74495, ChEBI:CHEBI:82748; EC=2.1.1.207;... | null | null | null | null | FUNCTION: Methylates the ribose at the nucleotide 34 wobble position in the two leucyl isoacceptors tRNA(Leu)(CmAA) and tRNA(Leu)(cmnm5UmAA). Catalyzes the methyl transfer from S-adenosyl-L-methionine to the 2'-OH of the wobble nucleotide. Recognition of the target requires a pyridine at position 34 and N(6)-(isopenten... | Escherichia coli (strain K12) |
P0AGJ9 | SYY_ECOLI | MASSNLIKQLQERGLVAQVTDEEALAERLAQGPIALYCGFDPTADSLHLGHLVPLLCLKRFQQAGHKPVALVGGATGLIGDPSFKAAERKLNTEETVQEWVDKIRKQVAPFLDFDCGENSAIAANNYDWFGNMNVLTFLRDIGKHFSVNQMINKEAVKQRLNREDQGISFTEFSYNLLQGYDFACLNKQYGVVLQIGGSDQWGNITSGIDLTRRLHQNQVFGLTVPLITKADGTKFGKTEGGAVWLDPKKTSPYKFYQFWINTADADVYRFLKFFTFMSIEEINALEEEDKNSGKAPRAQYVLAEQVTRLVHGEEGLQAA... | 6.1.1.1 | null | tRNA aminoacylation [GO:0043039]; tyrosyl-tRNA aminoacylation [GO:0006437] | cytosol [GO:0005829]; membrane [GO:0016020] | ATP binding [GO:0005524]; protein homodimerization activity [GO:0042803]; RNA binding [GO:0003723]; tyrosine-tRNA ligase activity [GO:0004831] | PF01479;PF00579; | 3.40.50.620;3.10.290.10;1.10.240.10; | Class-I aminoacyl-tRNA synthetase family, TyrS type 1 subfamily | PTM: Acetylated at Lys-144 (PubMed:18723842, PubMed:28741290). Acetylation at Lys-144 leads to slightly decreased activity (PubMed:28741290). In vitro, in the presence of acetyl-phosphate, can also be acetylated at Lys-67, Lys-85, Lys-90, Lys-230, Lys-235, Lys-238, Lys-321 and Lys-377. Acetylation at Lys-85, Lys-235 or... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02006, ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosine + tRNA(Tyr) = AMP + diphosphate + H(+) + L-tyrosyl-tRNA(Tyr); Xref=Rhea:RHEA:10220, Rhea:RHEA-COMP:9706, Rhea:RHEA-COMP:9707, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58315, ChEBI:CHEBI:78442, ChEBI:CHEBI:78536, ChEBI:CHEBI:456215; EC=6.1.1.1; Ev... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.027 mM for L-tyrosine {ECO:0000269|PubMed:4292198}; KM=0.0033 mM for L-tyrosine {ECO:0000269|PubMed:11006270}; KM=0.015 mM for D-tyrosine {ECO:0000269|PubMed:4292198}; KM=0.0177 mM for azatyrosine {ECO:0000269|PubMed:11006270}; KM=22 nM for tRNA(Tyr) (in the abse... | null | null | null | FUNCTION: Catalyzes the attachment of L-tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr) (PubMed:4292198, PubMed:4579631). Can also mischarge tRNA(Tyr) with D-tyrosine, leading to the formation of D-tyrosyl-tRNA(Tyr), ... | Escherichia coli (strain K12) |
P0AGK1 | UBIA_ECOLI | MEWSLTQNKLLAFHRLMRTDKPIGALLLLWPTLWALWVATPGVPQLWILAVFVAGVWLMRAAGCVVNDYADRKFDGHVKRTANRPLPSGAVTEKEARALFVVLVLISFLLVLTLNTMTILLSIAALALAWVYPFMKRYTHLPQVVLGAAFGWSIPMAFAAVSESVPLSCWLMFLANILWAVAYDTQYAMVDRDDDVKIGIKSTAILFGQYDKLIIGILQIGVLALMAIIGELNGLGWGYYWSILVAGALFVYQQKLIANREREACFKAFMNNNYVGLVLFLGLAMSYWHF | 2.5.1.39 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_01635, ECO:0000269|PubMed:4552989, ECO:0000269|PubMed:8155731}; Note=Can also use Mn(2+) and Co(2+) with lower efficiency. {ECO:0000269|PubMed:8155731}; | ubiquinone biosynthetic process [GO:0006744] | plasma membrane [GO:0005886] | 4-hydroxybenzoate decaprenyltransferase activity [GO:0002083]; 4-hydroxybenzoate nonaprenyltransferase activity [GO:0047293]; 4-hydroxybenzoate octaprenyltransferase activity [GO:0008412]; transferase activity, transferring alkyl or aryl (other than methyl) groups [GO:0016765] | PF01040; | 1.10.357.140;1.20.120.1780; | UbiA prenyltransferase family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_01635, ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:4552989, ECO:0000269|PubMed:8155731}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01635}. | CATALYTIC ACTIVITY: Reaction=4-hydroxybenzoate + all-trans-octaprenyl diphosphate = 4-hydroxy-3-all-trans-octaprenylbenzoate + diphosphate; Xref=Rhea:RHEA:27782, ChEBI:CHEBI:1617, ChEBI:CHEBI:17879, ChEBI:CHEBI:33019, ChEBI:CHEBI:57711; EC=2.5.1.39; Evidence={ECO:0000255|HAMAP-Rule:MF_01635, ECO:0000269|PubMed:4552989}... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=255 uM for GPP {ECO:0000269|PubMed:8155731}; KM=22 uM for FPP {ECO:0000269|PubMed:8155731}; KM=31 uM for SPP {ECO:0000269|PubMed:8155731}; | PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis. {ECO:0000255|HAMAP-Rule:MF_01635, ECO:0000269|PubMed:4552989}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.8. {ECO:0000269|PubMed:8155731}; | null | FUNCTION: Catalyzes the prenylation of para-hydroxybenzoate (PHB) with an all-trans polyprenyl group. Mediates the second step in the final reaction sequence of ubiquinone-8 (UQ-8) biosynthesis, which is the condensation of the polyisoprenoid side chain with PHB, generating the first membrane-bound Q intermediate 3-oct... | Escherichia coli (strain K12) |
P0AGM7 | URAA_ECOLI | MTRRAIGVSERPPLLQTIPLSLQHLFAMFGATVLVPVLFHINPATVLLFNGIGTLLYLFICKGKIPAYLGSSFAFISPVLLLLPLGYEVALGGFIMCGVLFCLVSFIVKKAGTGWLDVLFPPAAMGAIVAVIGLELAGVAAGMAGLLPAEGQTPDSKTIIISITTLAVTVLGSVLFRGFLAIIPILIGVLVGYALSFAMGIVDTTPIINAHWFALPTLYTPRFEWFAILTILPAALVVIAEHVGHLVVTANIVKKDLLRDPGLHRSMFANGLSTVISGFFGSTPNTTYGENIGVMAITRVYSTWVIGGAAIFAILLSCVG... | null | null | uracil import across plasma membrane [GO:0098721]; uracil transport [GO:0015857] | membrane [GO:0016020]; plasma membrane [GO:0005886] | protein homodimerization activity [GO:0042803]; uracil transmembrane transporter activity [GO:0015210]; uracil:monoatomic cation symporter activity [GO:0015505]; xanthine transmembrane transporter activity [GO:0042907] | PF00860; | null | Nucleobase:cation symporter-2 (NCS2) (TC 2.A.40) family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:21423164}; Multi-pass membrane protein {ECO:0000269|PubMed:21423164}. | CATALYTIC ACTIVITY: Reaction=H(+)(in) + uracil(in) = H(+)(out) + uracil(out); Xref=Rhea:RHEA:29239, ChEBI:CHEBI:15378, ChEBI:CHEBI:17568; Evidence={ECO:0000269|PubMed:21423164}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:29241; Evidence={ECO:0000269|PubMed:21423164}; | null | null | null | null | FUNCTION: Transport of uracil in the cell. {ECO:0000269|PubMed:21423164, ECO:0000269|PubMed:7721693}. | Escherichia coli (strain K12) |
P0C005 | ANOP_ANOSM | GLLKRIKTLL | null | null | defense response to bacterium [GO:0042742]; defense response to fungus [GO:0050832]; killing of cells of another organism [GO:0031640] | extracellular region [GO:0005576] | null | null | null | null | PTM: The C-terminal amidation is crucial for activity, since the carboxylated peptide has antimicrobial and mast cell degranulation activities drastically reduced compared to amidated peptide. However, the carboxylated peptide has no hemolytic activity, like the amidated peptide. {ECO:0000269|PubMed:17994639}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11006592}. | null | null | null | null | null | FUNCTION: Antimicrobial peptide that exhibits broad-spectrum antimicrobial activity against both Gram-positive and Gram-negative bacteria (PubMed:11738089, PubMed:15635634, PubMed:25530580). Also shows antifungal activities (PubMed:24472551). Exhibits potent activity in stimulating degranulation from rat peritoneal mas... | Anoplius samariensis (Solitary wasp) |
P0C018 | RL18_ECOLI | MDKKSARIRRATRARRKLQELGATRLVVHRTPRHIYAQVIAPNGSEVLVAASTVEKAIAEQLKYTGNKDAAAAVGKAVAERALEKGIKDVSFDRSGFQYHGRVQALADAAREAGLQF | null | null | cytoplasmic translation [GO:0002181] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; cytosolic large ribosomal subunit [GO:0022625] | 5S rRNA binding [GO:0008097]; structural constituent of ribosome [GO:0003735] | PF00861; | 3.30.420.100; | Universal ribosomal protein uL18 family | PTM: The protein has been shown to contain a phosphoserine, which was required for the protein to bind to 5S rRNA (PubMed:10529214). However, the presence of this phosphoserine is controversial, and it has not been seen by mass spectrometry. {ECO:0000269|PubMed:10529214}. | null | null | null | null | null | null | FUNCTION: This is one of the proteins that mediates the attachment of the 5S rRNA subcomplex onto the large ribosomal subunit where it forms part of the central protuberance. Binds stably to 5S rRNA; increases binding abilities of L5 in a cooperative fashion; both proteins together confer 23S rRNA binding. The 5S rRNA ... | Escherichia coli (strain K12) |
P0C023 | TX2B_MYRPI | LIGLVSKGTCVLVKTVCKKVLKQ | null | null | defense response to bacterium [GO:0042742]; killing of cells of another organism [GO:0031640] | extracellular region [GO:0005576] | toxin activity [GO:0090729] | null | null | Formicidae venom precursor-01 superfamily, Ant pilosulin family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15019477}. | null | null | null | null | null | FUNCTION: Heterodimer protein that may serve both defensive (pain-inducing) and predatory (insecticidal) roles (PubMed:28513074). Has membrane-disrupting activity and shows induction of non-specific calcium influx into cells, (PubMed:28513074). Shows broad-spectrum activity against a diverse range of bacteria, and cell... | Myrmecia pilosula (Jack jumper ant) (Australian jumper ant) |
P0C024 | NUDT7_HUMAN | MSRLGLPEEPVRNSLLDDAKARLRKYDIGGKYSHLPYNKYSVLLPLVAKEGKLHLLFTVRSEKLRRAPGEVCFPGGKRDPTDMDDAATALREAQEEVGLRPHQVEVVCCLVPCLIDTDTLITPFVGLIDHNFQAQPNPAEVKDVFLVPLAYFLHPQVHDQHYVTRLGHRFINHIFEYTNPEDGVTYQIKGMTANLAVLVAFIILEKKPTFEVQFNLNDVLASSEELFLKVHKKATSRL | 3.6.1.- | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:Q99P30}; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q99P30}; | acetyl-CoA catabolic process [GO:0046356]; brown fat cell differentiation [GO:0050873]; butyryl-CoA catabolic process [GO:0044580]; coenzyme A catabolic process [GO:0015938]; malonyl-CoA catabolic process [GO:2001294]; medium-chain fatty-acyl-CoA catabolic process [GO:0036114]; nucleoside diphosphate metabolic process ... | cytosol [GO:0005829]; peroxisomal matrix [GO:0005782]; peroxisome [GO:0005777] | coenzyme A diphosphatase activity [GO:0010945]; magnesium ion binding [GO:0000287]; manganese ion binding [GO:0030145]; snoRNA binding [GO:0030515] | PF00293; | 3.90.79.10; | Nudix hydrolase family, PCD1 subfamily | null | SUBCELLULAR LOCATION: Peroxisome {ECO:0000250|UniProtKB:Q99P30}. | CATALYTIC ACTIVITY: Reaction=H2O + hexanoyl-CoA = adenosine 3',5'-bisphosphate + 2 H(+) + hexanoyl-4'-phosphopantetheine; Xref=Rhea:RHEA:49980, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58343, ChEBI:CHEBI:62620, ChEBI:CHEBI:132012; Evidence={ECO:0000250|UniProtKB:Q99P30}; PhysiologicalDirection=left-to-right; X... | null | null | null | null | FUNCTION: Fatty acyl-coenzyme A (CoA) diphosphatase that hydrolyzes fatty acyl-CoA to yield acyl-4'-phosphopantetheine and adenosine 3',5'-bisphosphate (By similarity). Cleaves CoA, CoA esters and oxidized CoA with similar efficiencies (By similarity). Preferentially hydrolyzes medium-chain acyl-CoAs and bile acid-CoAs... | Homo sapiens (Human) |
P0C027 | NUD10_MOUSE | MKCKPNQTRTYDPEGFKKRAACLCFRSEREDEVLLVSSSRYPDRWIVPGGGMEPEEEPDGAAVREVYEEAGVKGKLGRLLGVFEQNQDRKHRTYVFVLTVTELLEDWEDSVSIGRKREWFKIEDAIKVLQCHKPVHAEYLEKLKLGGSPTNGNSAAPSPPESEP | 3.6.1.52; 3.6.1.60 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q8NFP7}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:Q8NFP7}; Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit. Mn(2+) may be the true cofactor in vivo. {ECO:0000250|UniProtKB:Q8NFP7}; | adenosine 5'-(hexahydrogen pentaphosphate) catabolic process [GO:1901911]; diadenosine hexaphosphate catabolic process [GO:1901909]; diadenosine pentaphosphate catabolic process [GO:1901907]; diphosphoinositol polyphosphate metabolic process [GO:0071543] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | bis(5'-adenosyl)-hexaphosphatase activity [GO:0034431]; bis(5'-adenosyl)-pentaphosphatase activity [GO:0034432]; diphosphoinositol-polyphosphate diphosphatase activity [GO:0008486]; endopolyphosphatase activity [GO:0000298]; metal ion binding [GO:0046872] | PF00293; | 3.90.79.10; | Nudix hydrolase family, DIPP subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8NFP7}. | CATALYTIC ACTIVITY: Reaction=diphospho-myo-inositol polyphosphate + H2O = myo-inositol polyphosphate + phosphate.; EC=3.6.1.52; Evidence={ECO:0000269|PubMed:12689335}; CATALYTIC ACTIVITY: Reaction=H2O + P(1),P(6)-bis(5'-adenosyl) hexaphosphate = adenosine 5'-pentaphosphate + AMP + 2 H(+); Xref=Rhea:RHEA:32047, ChEBI:CH... | null | null | null | null | FUNCTION: Cleaves a beta-phosphate from the diphosphate groups in PP-InsP5 (diphosphoinositol pentakisphosphate), suggesting that it may play a role in signal transduction. Also able to catalyze the hydrolysis of dinucleoside oligophosphates, with Ap6A and Ap5A being the preferred substrates. The major reaction product... | Mus musculus (Mouse) |
P0C028 | NUD11_MOUSE | MKCKPNQTRTYDPEGFKKRAACLCFRSEREDEVLLVSSSRYPDRWIVPGGGMEPEEEPDGAAVREVYEEAGVKGKLGRLLGVFEQNQDRKHRTYVFVLTVTELLEDWEDSVSIGRKREWFKIEDAIKVLQCHKPVHAEYLEKLKLGGSPTNGNSAAPSPPESEP | 3.6.1.52; 3.6.1.60 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q96G61}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:Q96G61}; Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit. Mn(2+) may be the true cofactor in vivo. {ECO:0000250|UniProtKB:Q96G61}; | adenosine 5'-(hexahydrogen pentaphosphate) catabolic process [GO:1901911]; diadenosine hexaphosphate catabolic process [GO:1901909]; diadenosine pentaphosphate catabolic process [GO:1901907]; diphosphoinositol polyphosphate metabolic process [GO:0071543] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | bis(5'-adenosyl)-hexaphosphatase activity [GO:0034431]; bis(5'-adenosyl)-pentaphosphatase activity [GO:0034432]; diphosphoinositol-polyphosphate diphosphatase activity [GO:0008486]; endopolyphosphatase activity [GO:0000298]; metal ion binding [GO:0046872] | PF00293; | 3.90.79.10; | Nudix hydrolase family, DIPP subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q96G61}. | CATALYTIC ACTIVITY: Reaction=diphospho-myo-inositol polyphosphate + H2O = myo-inositol polyphosphate + phosphate.; EC=3.6.1.52; Evidence={ECO:0000269|PubMed:12689335}; CATALYTIC ACTIVITY: Reaction=H2O + P(1),P(6)-bis(5'-adenosyl) hexaphosphate = adenosine 5'-pentaphosphate + AMP + 2 H(+); Xref=Rhea:RHEA:32047, ChEBI:CH... | null | null | null | null | FUNCTION: Cleaves a beta-phosphate from the diphosphate groups in PP-InsP5 (diphosphoinositol pentakisphosphate), suggesting that it may play a role in signal transduction. Also able to catalyze the hydrolysis of dinucleoside oligophosphates, with Ap6A and Ap5A being the preferred substrates. The major reaction product... | Mus musculus (Mouse) |
P0C037 | PPNP_ECOLI | MLQSNEYFSGKVKSIGFSSSSTGRASVGVMVEGEYTFSTAEPEEMTVISGALNVLLPDATDWQVYEAGSVFNVPGHSEFHLQVAEPTSYLCRYL | 2.4.2.1; 2.4.2.2 | null | null | cytosol [GO:0005829] | guanosine phosphorylase activity [GO:0047975]; protein homodimerization activity [GO:0042803]; purine-nucleoside phosphorylase activity [GO:0004731]; pyrimidine-nucleoside phosphorylase activity [GO:0016154]; thymidine phosphorylase activity [GO:0009032]; uridine phosphorylase activity [GO:0004850] | PF06865; | 2.60.120.10; | Nucleoside phosphorylase PpnP family | null | null | CATALYTIC ACTIVITY: Reaction=a purine D-ribonucleoside + phosphate = a purine nucleobase + alpha-D-ribose 1-phosphate; Xref=Rhea:RHEA:19805, ChEBI:CHEBI:26386, ChEBI:CHEBI:43474, ChEBI:CHEBI:57720, ChEBI:CHEBI:142355; EC=2.4.2.1; Evidence={ECO:0000269|PubMed:27941785}; CATALYTIC ACTIVITY: Reaction=adenosine + phosphate... | null | null | null | null | FUNCTION: Catalyzes the phosphorolysis of diverse nucleosides, yielding D-ribose 1-phosphate and the respective free bases. Can use uridine, adenosine, guanosine, cytidine, thymidine, inosine and xanthosine as substrates. Also catalyzes the reverse reactions. Is not able to produce D-ribose 1-phosphate from D-ribose an... | Escherichia coli (strain K12) |
P0C045 | F_HCV77 | MSTNPKPQRKKPNVTPTVAHRTSSSRVAVRSLVEFTCCRAGALDWVCARRGRLPSGRNLEVDVSLSPRHVGPRAGPGLSPGTLGPSMAMRVAGGRDGSCLPVALGLAGAPQTPGVGRAIWVRSSIPLRAASPTSWGTYRSSAPLLEALPGPWRMASGFWKTA | null | null | negative regulation of cytoskeleton organization [GO:0051494]; symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of RIG-I activity [GO:0039540]; virus-mediated perturbation of host defense response [GO:0019049] | host cell nucleus [GO:0042025]; host cell perinuclear region of cytoplasm [GO:0044220]; viral capsid [GO:0019028] | complement binding [GO:0001848]; enzyme binding [GO:0019899]; serpin family protein binding [GO:0097655]; small GTPase binding [GO:0031267]; structural molecule activity [GO:0005198]; zymogen binding [GO:0035375] | PF01543; | null | null | null | SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000269|PubMed:12810869}. Host cytoplasm, host perinuclear region {ECO:0000269|PubMed:12810869}. | null | null | null | null | null | FUNCTION: Contributes to the RIGI-mediated inhibition of type I interferon production. {ECO:0000269|PubMed:27404108}. | Hepatitis C virus genotype 1a (isolate H77) (HCV) |
P0C054 | IBPA_ECOLI | MRNFDLSPLYRSAIGFDRLFNHLENNQSQSNGGYPPYNVELVDENHYRIAIAVAGFAESELEITAQDNLLVVKGAHADEQKERTYLYQGIAERNFERKFQLAENIHVRGANLVNGLLYIDLERVIPEAKKPRRIEIN | null | null | negative regulation of translation [GO:0017148]; protein stabilization [GO:0050821]; response to heat [GO:0009408] | cytosol [GO:0005829] | identical protein binding [GO:0042802]; mRNA 5'-UTR binding [GO:0048027]; protein homodimerization activity [GO:0042803] | PF00011; | 2.60.40.790; | Small heat shock protein (HSP20) family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14702418}. | null | null | null | null | null | FUNCTION: Associates with aggregated proteins, together with IbpB, to stabilize and protect them from irreversible denaturation and extensive proteolysis during heat shock and oxidative stress. Aggregated proteins bound to the IbpAB complex are more efficiently refolded and reactivated by the ATP-dependent chaperone sy... | Escherichia coli (strain K12) |
P0C058 | IBPB_ECOLI | MRNFDLSPLMRQWIGFDKLANALQNAGESQSFPPYNIEKSDDNHYRITLALAGFRQEDLEIQLEGTRLSVKGTPEQPKEEKKWLHQGLMNQPFSLSFTLAENMEVSGATFVNGLLHIDLIRNEPEPIAAQRIAISERPALNS | null | null | protein stabilization [GO:0050821]; response to heat [GO:0009408]; stress response to copper ion [GO:1990169] | cytoplasm [GO:0005737] | identical protein binding [GO:0042802] | PF00011; | 2.60.40.790; | Small heat shock protein (HSP20) family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14702418}. | null | null | null | null | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Thermostable up to 50 degrees Celsius.; | FUNCTION: Associates with aggregated proteins, together with IbpA, to stabilize and protect them from irreversible denaturation and extensive proteolysis during heat shock and oxidative stress. Aggregated proteins bound to the IbpAB complex are more efficiently refolded and reactivated by the ATP-dependent chaperone sy... | Escherichia coli (strain K12) |
P0C077 | RELE_ECOLI | MAYFLDFDERALKEWRKLGSTVREQLKKKLVEVLESPRIEANKLRGMPDCYKIKLRSSGYRLVYQVIDEKVVVFVISVGKRERSEVYSEAVKRIL | 3.1.-.- | null | cellular response to amino acid starvation [GO:0034198]; mRNA catabolic process [GO:0006402]; negative regulation of translation [GO:0017148]; regulation of DNA-templated transcription [GO:0006355]; regulation of growth [GO:0040008]; response to antibiotic [GO:0046677]; single-species biofilm formation [GO:0044010] | protein-DNA complex [GO:0032993]; toxin-antitoxin complex [GO:0110001] | DNA-binding transcription repressor activity [GO:0001217]; ribosome binding [GO:0043022]; RNA endonuclease activity [GO:0004521]; rRNA binding [GO:0019843]; toxin sequestering activity [GO:0097351]; transcription cis-regulatory region binding [GO:0000976] | PF05016; | 3.30.2310.20; | RelE toxin family | null | null | null | null | null | null | null | FUNCTION: Toxic component of a type II toxin-antitoxin (TA) system (PubMed:9767574). A sequence-specific, ribosome-dependent mRNA endoribonuclease that inhibits translation during amino acid starvation (the stringent response). In vitro acts by cleaving mRNA with high codon specificity in the ribosomal A site between p... | Escherichia coli (strain K12) |
P0C079 | RELB_ECOLI | MGSINLRIDDELKARSYAALEKMGVTPSEALRLMLEYIADNERLPFKQTLLSDEDAELVEIVKERLRNPKPVRVTLDEL | null | null | DNA-templated transcription [GO:0006351]; regulation of DNA-templated transcription [GO:0006355]; regulation of growth [GO:0040008]; single-species biofilm formation [GO:0044010] | protein-DNA complex [GO:0032993]; toxin-antitoxin complex [GO:0110001] | DNA-binding transcription repressor activity [GO:0001217]; toxin sequestering activity [GO:0097351]; transcription cis-regulatory region binding [GO:0000976] | PF04221; | 1.10.1220.10; | RelB/DinJ antitoxin family | PTM: Probably degraded by Lon protease during amino acid starvation (PubMed:11717402). Degraded in vitro by Lon (PubMed:19747491). {ECO:0000269|PubMed:11717402, ECO:0000269|PubMed:19747491}. | null | null | null | null | null | null | FUNCTION: Antitoxin component of a type II toxin-antitoxin (TA) system. Counteracts the effect of cognate toxin RelE via direct protein-protein interaction, preventing RelE from entering the ribosome A site and thus inhibiting its endoribonuclease activity. An autorepressor of relBE operon transcription. 2 RelB dimers ... | Escherichia coli (strain K12) |
P0C089 | PTPM1_RAT | MAASAWLEAGLARVLFYPTLLYTVFRGRVGGPAHRDWYHRIDHTVLLGALPLRSMTRRLVLDENVRGVITMNEEYETRFLCNTSKEWKNVGVEQLRLSTVDMTGVPTLANLHRGVQFALKYQSLGQCVYVHCKAGRSRSATMVAAYLIQVHNWSPEEAIEAIAKIRSHISIRPSQLEILKEFHKEIAARAAKN | 3.1.3.16; 3.1.3.27; 3.1.3.48 | null | cardiolipin biosynthetic process [GO:0032049]; dephosphorylation [GO:0016311]; negative regulation of insulin secretion involved in cellular response to glucose stimulus [GO:0061179]; regulation of intrinsic apoptotic signaling pathway [GO:2001242] | mitochondrial inner membrane [GO:0005743]; mitochondrion [GO:0005739] | myosin phosphatase activity [GO:0017018]; phosphatidylglycerophosphatase activity [GO:0008962]; phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity [GO:0004439]; protein tyrosine phosphatase activity [GO:0004725]; protein tyrosine/serine/threonine phosphatase activity [GO:0008138] | PF00782; | 3.90.190.10; | Protein-tyrosine phosphatase family, Non-receptor class dual specificity subfamily | null | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:16039589}; Peripheral membrane protein {ECO:0000269|PubMed:16039589}; Matrix side {ECO:0000269|PubMed:16039589}. | CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU10044}; PhysiologicalDir... | null | PATHWAY: Phospholipid metabolism; phosphatidylglycerol biosynthesis; phosphatidylglycerol from CDP-diacylglycerol: step 2/2. {ECO:0000250|UniProtKB:Q66GT5}. | null | null | FUNCTION: Lipid phosphatase which dephosphorylates phosphatidylglycerophosphate (PGP) to phosphatidylglycerol (PG) (By similarity). PGP is an essential intermediate in the biosynthetic pathway of cardiolipin, a mitochondrial-specific phospholipid regulating the membrane integrity and activities of the organelle (By sim... | Rattus norvegicus (Rat) |
P0C090 | RC3H2_MOUSE | MPVQAAQWTEFLSCPICYNEFDENVHKPISLGCSHTVCKTCLNKLHRKACPFDQTAINTDIDVLPVNFALLQLVGAQVPDHQSIKLSNLGENKHYEVAKKCVEDLALYLKPLSGGKGVASLNQSALSRPMQRKLVTLVNCQLVEEEGRVRAMRAARSLGERTVTELILQHQNPQQLSANLWAAVRARGCQFLGPAMQEEALKLVLLALEDGSALSRKVLVLFVVQRLEPRFPQASKTSIGHVVQLLYRASCFKVTKRDEDSSLMQLKEEFRSYEALRREHDAQIVHIAMEAGLRISPEQWSSLLYGDLAHKSHMQSIIDK... | 2.3.2.27 | null | B cell homeostasis [GO:0001782]; limb development [GO:0060173]; lung alveolus development [GO:0048286]; lymph node development [GO:0048535]; multicellular organism growth [GO:0035264]; negative regulation of T-helper 17 cell differentiation [GO:2000320]; nuclear-transcribed mRNA catabolic process, deadenylation-depende... | cell surface [GO:0009986]; cytoplasmic stress granule [GO:0010494]; intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020]; P-body [GO:0000932] | DNA binding [GO:0003677]; double-stranded RNA binding [GO:0003725]; metal ion binding [GO:0046872]; mRNA binding [GO:0003729]; RNA stem-loop binding [GO:0035613]; ubiquitin protein ligase activity [GO:0061630] | PF18386;PF21206;PF00642;PF14634; | 1.20.120.1790;4.10.1000.10;3.30.40.10; | null | PTM: Proteolytically cleaved by MALT1 in activated CD4(+) T cells; cleavage at Arg-509 is critical for promoting RC3H1 degradation in response to T-cell receptor (TCR) stimulation, and hence is necessary for prolonging the stability of a set of mRNAs controlling Th17 cell differentiation. {ECO:0000269|PubMed:25282160}. | SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000269|PubMed:23583642}. Note=During stress, such as that induced by arsenite, localizes to cytosolic stress granules. Localization to stress granules, but not to P-bodies, depends upon the RING-type zinc finger. | CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; Evidence={ECO:0000250|UniProtKB:Q9HBD1}; | null | PATHWAY: Protein modification; protein ubiquitination. {ECO:0000250|UniProtKB:Q9HBD1}. | null | null | FUNCTION: Post-transcriptional repressor of mRNAs containing a conserved stem loop motif, called constitutive decay element (CDE), which is often located in the 3'-UTR, as in HMGXB3, ICOS, IER3, NFKBID, NFKBIZ, PPP1R10, TNF and in many more mRNAs. Binds to CDE and promotes mRNA deadenylation and degradation. This proce... | Mus musculus (Mouse) |
P0C092 | CSEN4_MOUSE | MRQLPAGPSSLACSGCKAGRLVTVPFSSRDAEDQGSREGIGWQPPGRSWAHTTEQEGKHQVAKATVHPPGPDALLLNQVDPVQCCPTRL | null | null | behavioral response to pain [GO:0048266]; intracellular protein transport [GO:0006886]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of transcription by RNA polymerase II [GO:0000122]; potassium ion transport [GO:0006813]; regulation of neuron apoptotic process [GO:0043523]; regu... | axon [GO:0030424]; axon terminus [GO:0043679]; cytosol [GO:0005829]; dendrite [GO:0030425]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; protein-DNA complex [GO:0032993]; voltage-gated potassium channel complex [GO:0008076] | calcium ion binding [GO:0005509]; calcium-dependent protein binding [GO:0048306]; DNA binding [GO:0003677]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; potassium channel regulator activity [GO:0015459]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:... | null | null | null | null | null | null | null | null | null | null | FUNCTION: Unknown for isoform 4. Csen is involved in calcium-dependent transcriptional repression, regulation of potassium channels, and perhaps in processing of PSEN2 and apoptosis. | Mus musculus (Mouse) |
P0C093 | SLMA_ECOLI | MAEKQTAKRNRREEILQSLALMLESSDGSQRITTAKLAASVGVSEAALYRHFPSKTRMFDSLIEFIEDSLITRINLILKDEKDTTARLRLIVLLLLGFGERNPGLTRILTGHALMFEQDRLQGRINQLFERIEAQLRQVLREKRMREGEGYTTDETLLASQILAFCEGMLSRFVRSEFKYRPTDDFDARWPLIAAQLQ | null | null | division septum site selection [GO:0000918]; negative regulation of division septum assembly [GO:0010974]; negative regulation of protein polymerization [GO:0032272]; regulation of DNA-templated transcription [GO:0006355] | bacterial nucleoid [GO:0043590]; cytoplasm [GO:0005737] | DNA binding [GO:0003677]; DNA-binding transcription factor activity [GO:0003700]; identical protein binding [GO:0042802]; protein homodimerization activity [GO:0042803]; sequence-specific DNA binding [GO:0043565]; transcription cis-regulatory region binding [GO:0000976] | PF00440; | 1.10.357.10; | Nucleoid occlusion factor SlmA family | null | SUBCELLULAR LOCATION: Cytoplasm, nucleoid {ECO:0000255|HAMAP-Rule:MF_01839, ECO:0000269|PubMed:15916962}. | null | null | null | null | null | FUNCTION: Required for nucleoid occlusion (NO) phenomenon, which prevents Z-ring formation and cell division over the nucleoid. Acts as a DNA-associated cell division inhibitor that binds simultaneously chromosomal DNA and FtsZ, and disrupts the assembly of FtsZ polymers. SlmA-DNA-binding sequences (SBS) are dispersed ... | Escherichia coli (strain K12) |
P0C0A3 | CHMP6_MOUSE | MGNLFGRKKQSRVTEQDRAILQLKQQRDKLRQYQKRVTQQLERERALARQLLRDGRKERAKLLLKKKRYREQLLDRTENQISSLEAMVQSIEFTQIEMKVMEGLQVGNECLNKMHQVMSIEEVERILDETQEAVEYQRQIDELLAGNFTQEDEDAILEELNAITQEQMELPEVPSEPLPDRNPEAPAKARSRQAELVAAS | null | null | autophagosome maturation [GO:0097352]; autophagy [GO:0006914]; late endosome to lysosome transport [GO:1902774]; late endosome to vacuole transport via multivesicular body sorting pathway [GO:0032511]; membrane fission [GO:0090148]; midbody abscission [GO:0061952]; mitotic metaphase chromosome alignment [GO:0007080]; m... | amphisome membrane [GO:1904930]; autophagosome membrane [GO:0000421]; ESCRT III complex [GO:0000815]; kinetochore [GO:0000776]; kinetochore microtubule [GO:0005828]; lysosomal membrane [GO:0005765]; midbody [GO:0030496]; multivesicular body [GO:0005771]; multivesicular body membrane [GO:0032585]; nuclear pore [GO:00056... | protein-containing complex binding [GO:0044877] | PF03357; | 1.10.287.1060; | SNF7 family | PTM: ISGylated in a CHMP5-dependent manner. Isgylation weakens its interaction with VPS4A (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Endomembrane system {ECO:0000250}. Endosome membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. Late endosome membrane {ECO:0000250}. Membrane {ECO:0000250|UniProtKB:Q96FZ7}; Lipid-anchor {ECO:0000250|UniProtKB:Q96FZ7}. Note=Localizes to endosomal membranes. {ECO:0000250}. | null | null | null | null | null | FUNCTION: Probable core component of the endosomal sorting required for transport complex III (ESCRT-III) which is involved in multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limi... | Mus musculus (Mouse) |
P0C0A9 | SVIP_RAT | MGLCFPCPAESAPPSPSPEEKRAKLAEAAERRQKEAASRGILDIQSVEAKKKKKEQLEKQMETSGPPAGGLRWTVS | null | null | negative regulation of ERAD pathway [GO:1904293]; negative regulation of protein-containing complex assembly [GO:0031333]; negative regulation of retrograde protein transport, ER to cytosol [GO:1904153]; negative regulation of ubiquitin-dependent protein catabolic process [GO:2000059]; negative regulation of VCP-NPL4-U... | endoplasmic reticulum membrane [GO:0005789]; Golgi membrane [GO:0000139]; membrane [GO:0016020]; plasma membrane [GO:0005886]; smooth endoplasmic reticulum membrane [GO:0030868] | ATPase binding [GO:0051117]; protein self-association [GO:0043621] | PF15811; | null | SVIP family | null | SUBCELLULAR LOCATION: Smooth endoplasmic reticulum membrane; Peripheral membrane protein. Golgi apparatus membrane; Peripheral membrane protein. Cell membrane; Peripheral membrane protein. Membrane {ECO:0000250|UniProtKB:Q8NHG7}; Lipid-anchor {ECO:0000250|UniProtKB:Q8NHG7}. | null | null | null | null | null | FUNCTION: Overexpression causes the formation of large vacuoles that seemed to be derived from the endoplasmic reticulum. {ECO:0000269|PubMed:12529442}. | Rattus norvegicus (Rat) |
P0C0F6 | RPFC_XANCP | MKSPLPWLKRRLSGRADSEHAQNLIRIIITTLFISYLGWRYQHTHGDTLMATWLILVGELLVSLGLMVAILLRPQVSHTRRLIGMLLDYTCTGAIMAIQGEPASPLYAVCMWVTIGNGLRYGSNYLRAATAMGSLCFLGAILISPYWKANPYLSWGLLLGLIAVPLYFDSLLRAMTRAVREARHANQAKSRFLANMSHEFRTPLNGLSGMTEVLATTRLDAEQKECLNTIQASARSLLSLVEEVLDISAIEAGKIRIDRRDFSLREMIGSVNLILQPQARGRRLEYGTQVADDVPDLLKGDTAHLRQVLLNLVGNAVKFT... | 2.7.13.3 | null | cellular hyperosmotic response [GO:0071474] | plasma membrane [GO:0005886] | ATP binding [GO:0005524]; histidine phosphotransfer kinase activity [GO:0009927]; phosphorelay sensor kinase activity [GO:0000155] | PF02518;PF00512;PF01627;PF00072; | 1.10.287.130;3.40.50.2300;3.30.565.10;1.20.120.160; | null | PTM: Autophosphorylated (By similarity). Activation may require a sequential transfer of a phosphate group from a His in the primary transmitter domain, to an Asp in the receiver domain and to a His in the secondary transmitter domain (Probable). {ECO:0000250|UniProtKB:P0C0F7, ECO:0000305}. | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}. Note=Localizes at the cell poles. {ECO:0000250|UniProtKB:P0C0F7}. | CATALYTIC ACTIVITY: Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.; EC=2.7.13.3; Evidence={ECO:0000250|UniProtKB:P0C0F7}; | null | null | null | null | FUNCTION: Hybrid sensor kinase that regulates diverse biological functions through two distinct molecular mechanisms (By similarity). At low cell density, the extracellular concentration of the diffusible signaling factor (DSF) is below a threshold, and unphosphorylated RpfC is involved in the negative regulation of DS... | Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25) |
P0C0F7 | RPFC_XANC8 | MKSPLPWLKRRLSGRADSEHAQNLIRIIITTLFISYLGWRYQHTHGDTLMATWLILVGELLVSLGLMVAILLRPQVSHTRRLIGMLLDYTCTGAIMAIQGEPASPLYAVCMWVTIGNGLRYGSNYLRAATAMGSLCFLGAILISPYWKANPYLSWGLLLGLIAVPLYFDSLLRAMTRAVREARHANQAKSRFLANMSHEFRTPLNGLSGMTEVLATTRLDAEQKECLNTIQASARSLLSLVEEVLDISAIEAGKIRIDRRDFSLREMIGSVNLILQPQARGRRLEYGTQVADDVPDLLKGDTAHLRQVLLNLVGNAVKFT... | 2.7.13.3 | null | cellular hyperosmotic response [GO:0071474] | plasma membrane [GO:0005886] | ATP binding [GO:0005524]; phosphorelay sensor kinase activity [GO:0000155] | PF02518;PF00512;PF01627;PF00072; | 1.10.287.130;3.40.50.2300;3.30.565.10;1.20.120.160; | null | PTM: Autophosphorylated (PubMed:28369120). Activation may require a sequential transfer of a phosphate group from a His in the primary transmitter domain, to an Asp in the receiver domain and to a His in the secondary transmitter domain (Probable). {ECO:0000269|PubMed:28369120, ECO:0000305}. | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305|PubMed:28369120}; Multi-pass membrane protein {ECO:0000255}. Note=Localizes at the cell poles. {ECO:0000269|PubMed:20231439}. | CATALYTIC ACTIVITY: Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.; EC=2.7.13.3; Evidence={ECO:0000305|PubMed:28369120}; | null | null | null | null | FUNCTION: Hybrid sensor kinase that regulates diverse biological functions through two distinct molecular mechanisms (PubMed:16940295). At low cell density, the extracellular concentration of the diffusible signaling factor (DSF) is below a threshold, and unphosphorylated RpfC is involved in the negative regulation of ... | Xanthomonas campestris pv. campestris (strain 8004) |
P0C0G6 | G3P_STRPY | MVVKVGINGFGRIGRLAFRRIQNIEGVEVTRINDLTDPNMLAHLLKYDTTQGRFDGTVEVKEGGFEVNGNFIKVSAERDPENIDWATDGVEIVLEATGFFAKKEAAEKHLHANGAKKVVITAPGGNDVKTVVFNTNHDILDGTETVISGASCTTNCLAPMAKALHDAFGIQKGLMTTIHAYTGDQMILDGPHRGGDLRRARAGAANIVPNSTGAAKAIGLVIPELNGKLDGAAQRVPVPTGSVTELVVTLDKNVSVDEINSAMKAASNDSFGYTEDPIVSSDIVGVSYGSLFDATQTKVMEVDGSQLVKVVSWYDNEMSY... | 1.2.1.12 | null | glucose metabolic process [GO:0006006]; glycolytic process [GO:0006096]; NADH regeneration [GO:0006735] | cytoplasm [GO:0005737] | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity [GO:0004365]; NAD binding [GO:0051287]; NADP binding [GO:0050661]; protease binding [GO:0002020] | PF02800;PF00044; | 3.40.50.720; | Glyceraldehyde-3-phosphate dehydrogenase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=D-glyceraldehyde 3-phosphate + NAD(+) + phosphate = (2R)-3-phospho-glyceroyl phosphate + H(+) + NADH; Xref=Rhea:RHEA:10300, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57540, ChEBI:CHEBI:57604, ChEBI:CHEBI:57945, ChEBI:CHEBI:59776; EC=1.2.1.12; Evidence={ECO:0000250|UniProtKB:P09124}; | null | PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 1/5. {ECO:0000305}. | null | null | FUNCTION: Also binds human plasminogen.; FUNCTION: Catalyzes the oxidative phosphorylation of glyceraldehyde 3-phosphate (G3P) to 1,3-bisphosphoglycerate (BPG) using the cofactor NAD. The first reaction step involves the formation of a hemiacetal intermediate between G3P and a cysteine residue, and this hemiacetal inte... | Streptococcus pyogenes |
P0C0H6 | IMDH_STRPY | MSNWDTKFLKKGYTFDDVLLIPAESHVLPNEVDLKTKLADNLTLNIPIITAAMDTVTGSKMAIAIARAGGLGVIHKNMSITEQAEEVRKVKRSENGVIIDPFFLTPEHKVSEAEELMQRYRISGVPIVETLANRKLVGIITNRDMRFISDYNAPISEHMTSEHLVTAAVGTDLETAERILHEHRIEKLPLVDNSGRLSGLITIKDIEKVIEFPHAAKDEFGRLLVAAAVGVTSDTFERAEALFEAGADAIVIDTAHGHSAGVLRKIAEIRAHFPNRTLIAGNIATAEGARALYDAGVDVVKVGIGPGSICTTRVVAGVGV... | 1.1.1.205 | COFACTOR: Name=K(+); Xref=ChEBI:CHEBI:29103; Evidence={ECO:0000255|HAMAP-Rule:MF_01964}; | GMP biosynthetic process [GO:0006177]; GTP biosynthetic process [GO:0006183] | cytoplasm [GO:0005737] | IMP dehydrogenase activity [GO:0003938]; metal ion binding [GO:0046872]; nucleotide binding [GO:0000166] | PF00571;PF00478; | 3.20.20.70; | IMPDH/GMPR family | null | null | CATALYTIC ACTIVITY: Reaction=H2O + IMP + NAD(+) = H(+) + NADH + XMP; Xref=Rhea:RHEA:11708, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57464, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58053; EC=1.1.1.205; Evidence={ECO:0000255|HAMAP-Rule:MF_01964}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=62 uM for Inosine 5'-phosphate {ECO:0000269|PubMed:10200156}; KM=1180 uM for NAD(+) {ECO:0000269|PubMed:10200156}; | PATHWAY: Purine metabolism; XMP biosynthesis via de novo pathway; XMP from IMP: step 1/1. {ECO:0000255|HAMAP-Rule:MF_01964}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.8. {ECO:0000269|PubMed:10200156}; | null | FUNCTION: Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth. {ECO:0000255|HAMAP-Rule:MF_01964}. | Streptococcus pyogenes |
P0C0J0 | SPEB_STRPY | MNKKKLGIRLLSLLALGGFVLANPVFADQNFARNEKEAKDSAITFIQKSAAIKAGARSAEDIKLDKVNLGGELSGSNMYVYNISTGGFVIVSGDKRSPEILGYSTSGSFDANGKENIASFMESYVEQIKENKKLDTTYAGTAEIKQPVVKSLLDSKGIHYNQGNPYNLLTPVIEKVKPGEQSFVGQHAATGCVATATAQIMKYHNYPNKGLKDYTYTLSSNNPYFNHPKNLFAAISTRQYNWNNILPTYSGRESNVQKMAISELMADVGISVDMDYGPSSGSAGSSRVQRALKENFGYNQSVHQINRSDFSKQDWEAQID... | 3.4.22.10 | null | evasion of host immune response [GO:0042783]; proteolysis [GO:0006508]; symbiont-induced defense-related programmed cell death [GO:0034050]; symbiont-mediated suppression of host autophagy [GO:0140321] | extracellular region [GO:0005576]; host cell cytosol [GO:0044164]; host extracellular space [GO:0043655] | cysteine-type endopeptidase activity [GO:0004197]; cysteine-type peptidase activity [GO:0008234]; toxin activity [GO:0090729] | PF13734;PF01640; | 3.90.70.50; | Peptidase C10 family | PTM: The mature protease is derived from the precursor sequence by cleavage, either in cis via an autocatalytic mechanism, or in trans by mature SpeB, host trypsin or host subtilisin (PubMed:10429198, PubMed:8675287). Maturation can involve a number of protein cleavage intermediates (PubMed:10429198). Mature SpeB proba... | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:2198264}. Host extracellular space {ECO:0000250|UniProtKB:P0C0J1}. Host cytoplasm {ECO:0000250|UniProtKB:P0C0J1}. | CATALYTIC ACTIVITY: Reaction=Preferential cleavage with hydrophobic residues at P2, P1 and P1'.; EC=3.4.22.10; Evidence={ECO:0000269|PubMed:10429198, ECO:0000269|PubMed:11553627, ECO:0000269|PubMed:22645124, ECO:0000269|PubMed:7689226}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=246.6 uM for a substrate peptide {ECO:0000269|PubMed:22645124}; Note=kcat is 0.69 sec(-1) for a peptide. {ECO:0000269|PubMed:22645124}; | null | null | null | FUNCTION: Cysteine protease that acts as a key streptococcal virulence factor by cleaving host proteins involved in immune response (PubMed:10429198, PubMed:11553627, PubMed:1987034, PubMed:22645124, PubMed:8675287, PubMed:9169486, PubMed:9864206). Triggers inflammation by mediating cleavage of host proteins, which can... | Streptococcus pyogenes |
P0C0J1 | SPEB_STRP1 | MNKKKLGVRLLSLLALGGFVLANPVFADQNFARNEKEAKDSAITFIQKSAAIKAGARSAEDIKLDKVNLGGELSGSNMYVYNISTGGFVIVSGDKRSPEILGYSTSGSFDANGKENIASFMESYVEQIKENKKLDTTYAGTAEIKQPVVKSLLDSKGIHYNQGNPYNLLTPVIEKVKPGEQSFVGQHAATGCVATATAQIMKYHNYPNKGLKDYTYTLSSNNPYFNHPKNLFAAISTRQYNWNNILPTYSGRESNVQKMAISELMADVGISVDMDYGPSSGSAGSSRVQRALKENFGYNQSVHQINRGDFSKQDWEAQID... | 3.4.22.10 | null | evasion of host immune response [GO:0042783]; protein maturation [GO:0051604]; proteolysis [GO:0006508]; symbiont-induced defense-related programmed cell death [GO:0034050]; symbiont-mediated suppression of host autophagy [GO:0140321] | cytosol [GO:0005829]; extracellular region [GO:0005576]; host cell cytosol [GO:0044164]; host extracellular space [GO:0043655] | cysteine-type endopeptidase activity [GO:0004197]; toxin activity [GO:0090729] | PF13734;PF01640; | 3.90.70.50; | Peptidase C10 family | PTM: The mature protease is derived from the precursor sequence by cleavage, either in cis via an autocatalytic mechanism, or in trans by mature SpeB or host proteases (trypsin, plasmin or subtilisin) (PubMed:12621045). Maturation can involve a number of protein cleavage intermediates (PubMed:12621045). Mature SpeB pro... | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:7516997}. Host extracellular space {ECO:0000269|PubMed:18160402, ECO:0000269|PubMed:7516997}. Host cytoplasm {ECO:0000269|PubMed:35545676}. | CATALYTIC ACTIVITY: Reaction=Preferential cleavage with hydrophobic residues at P2, P1 and P1'.; EC=3.4.22.10; Evidence={ECO:0000269|PubMed:12621045, ECO:0000269|PubMed:19237546, ECO:0000269|PubMed:24331465, ECO:0000269|PubMed:28331908, ECO:0000269|PubMed:35110732, ECO:0000269|PubMed:35545676}; | null | null | null | null | FUNCTION: Cysteine protease that acts as a key streptococcal virulence factor by cleaving host proteins involved in immune response (PubMed:10456871, PubMed:11406581, PubMed:11598100, PubMed:12438337, PubMed:12621045, PubMed:19237546, PubMed:23532847, PubMed:24331465, PubMed:35008838, PubMed:35110732, PubMed:35545676, ... | Streptococcus pyogenes serotype M1 |
P0C0K3 | SRKA_ECOLI | MNNSAFTFQTLHPDTIMDALFEHGIRVDSGLTPLNSYENRVYQFQDEDRRRFVVKFYRPERWTADQILEEHQFALQLVNDEVPVAAPVAFNGQTLLNHQGFYFAVFPSVGGRQFEADNIDQMEAVGRYLGRMHQTGRKQLFIHRPTIGLNEYLIEPRKLFEDATLIPSGLKAAFLKATDELIAAVTAHWREDFTVLRLHGDCHAGNILWRDGPMFVDLDDARNGPAVQDLWMLLNGDKAEQRMQLETIIEAYEEFSEFDTAEIGLIEPLRAMRLVYYLAWLMRRWADPAFPKNFPWLTGEDYWLRQTATFIEQAKVLQEP... | 2.7.11.1 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305|PubMed:17302814}; Note=May bind 2 Mg(2+) ions. {ECO:0000305|PubMed:17302814}; | phosphorylation [GO:0016310] | cytoplasm [GO:0005737] | ATP binding [GO:0005524]; magnesium ion binding [GO:0000287]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF01636; | 1.20.1270.170;3.30.200.70;1.10.510.10; | SrkA/RdoA protein kinase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01497, ECO:0000305|PubMed:17302814}. | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000255|HAMAP-Rule:MF_01497, ECO:00... | null | null | null | null | FUNCTION: A protein kinase that (auto)phosphorylates on Ser and Thr residues (PubMed:17302814). Probably acts to suppress the effects of stress linked to accumulation of reactive oxygen species. Protects cells from stress by antagonizing the MazE-MazF TA module, probably indirectly as it has not been seen to phosphoryl... | Escherichia coli (strain K12) |
P0C0K5 | HAVR2_RAT | MFSWLPFSCALLLLQPLPARSLENAYTAEVGKNAYLPCSYTVPAPGTLVPICWGKGSCPLLQCASVVLRTDETNVTYRKSRRYQLKGNFYKGDMSLTIKNVTLADSGTYCCRIQFPGPMNDEKLELKLSITEPAKVIPAGTAHGDSTTASPRTLTTEGSGSETQTLVTLHDNNGTKISTWADEIKDSGETIRTAVHIGVGVSAGLALALILGVLILKWYSSKKKKLQDLSLITLANSPPGGLVNAGAGRIRSEENIYTIEENIYEMENSNEYYCYVSSQQPS | null | null | adaptive immune response [GO:0002250]; cellular response to lipopolysaccharide [GO:0071222]; defense response to Gram-positive bacterium [GO:0050830]; inflammatory response [GO:0006954]; innate immune response [GO:0045087]; macrophage activation involved in immune response [GO:0002281]; maternal process involved in fem... | anchoring junction [GO:0070161]; cell surface [GO:0009986]; early endosome [GO:0005769]; immunological synapse [GO:0001772]; mediator complex [GO:0016592] | metal ion binding [GO:0046872] | PF07686; | 2.60.40.10; | Immunoglobulin superfamily, TIM family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Cell junction {ECO:0000250|UniProtKB:Q8TDQ0}. Note=Localizes to the immunological synapse between CD8+ T-cells and target cells. {ECO:0000250|UniProtKB:Q8TDQ0}. | null | null | null | null | null | FUNCTION: Cell surface receptor implicated in modulating innate and adaptive immune responses. Generally accepted to have an inhibiting function. Reports on stimulating functions suggest that the activity may be influenced by the cellular context and/or the respective ligand. Regulates macrophage activation. Inhibits T... | Rattus norvegicus (Rat) |
P0C0L2 | OSMC_ECOLI | MTIHKKGQAHWEGDIKRGKGTVSTESGVLNQQPYGFNTRFEGEKGTNPEELIGAAHAACFSMALSLMLGEAGFTPTSIDTTADVSLDKVDAGFAITKIALKSEVAVPGIDASTFDGIIQKAKAGCPVSQVLKAEITLDYQLKS | 1.11.1.- | null | hyperosmotic response [GO:0006972]; response to hydroperoxide [GO:0033194]; response to oxidative stress [GO:0006979] | cytosol [GO:0005829] | peroxidase activity [GO:0004601]; peroxiredoxin activity [GO:0051920]; protein homodimerization activity [GO:0042803] | PF02566; | 3.30.300.20; | OsmC/Ohr family | null | SUBCELLULAR LOCATION: Cytoplasm. | CATALYTIC ACTIVITY: Reaction=[protein]-dithiol + a hydroperoxide = [protein]-disulfide + an alcohol + H2O; Xref=Rhea:RHEA:10008, Rhea:RHEA-COMP:10593, Rhea:RHEA-COMP:10594, ChEBI:CHEBI:15377, ChEBI:CHEBI:29950, ChEBI:CHEBI:30879, ChEBI:CHEBI:35924, ChEBI:CHEBI:50058; | null | null | null | null | FUNCTION: Preferentially metabolizes organic hydroperoxides over inorganic hydrogen peroxide. {ECO:0000269|PubMed:14627744}. | Escherichia coli (strain K12) |
P0C0L4 | CO4A_HUMAN | MRLLWGLIWASSFFTLSLQKPRLLLFSPSVVHLGVPLSVGVQLQDVPRGQVVKGSVFLRNPSRNNVPCSPKVDFTLSSERDFALLSLQVPLKDAKSCGLHQLLRGPEVQLVAHSPWLKDSLSRTTNIQGINLLFSSRRGHLFLQTDQPIYNPGQRVRYRVFALDQKMRPSTDTITVMVENSHGLRVRKKEVYMPSSIFQDDFVIPDISEPGTWKISARFSDGLESNSSTQFEVKKYVLPNFEVKITPGKPYILTVPGHLDEMQLDIQARYIYGKPVQGVAYVRFGLLDEDGKKTFFRGLESQTKLVNGQSHISLSKAEFQ... | null | null | complement activation [GO:0006956]; complement activation, classical pathway [GO:0006958]; inflammatory response [GO:0006954]; innate immune response [GO:0045087]; positive regulation of apoptotic cell clearance [GO:2000427] | axon [GO:0030424]; blood microparticle [GO:0072562]; dendrite [GO:0030425]; endoplasmic reticulum lumen [GO:0005788]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; neuronal cell body [GO:0043025]; plasma membrane [GO:0005886]; synapse [GO:0045202] | complement component C1q complex binding [GO:0001849]; endopeptidase inhibitor activity [GO:0004866] | PF00207;PF07703;PF07677;PF01821;PF21145;PF01835;PF17791;PF17789;PF01759;PF07678; | 1.50.10.20;2.20.130.20;2.40.50.120;2.60.120.1540;2.60.40.1930;2.60.40.1940;6.20.50.160;2.60.40.690;1.20.91.20;2.60.40.10; | null | PTM: Prior to secretion, the single-chain precursor is enzymatically cleaved to yield non-identical chains alpha, beta and gamma. During activation, the alpha chain is cleaved by C1 into C4a and C4b, and C4b stays linked to the beta and gamma chains. Further degradation of C4b by C1 into the inactive fragments C4c and ... | SUBCELLULAR LOCATION: Secreted. Synapse {ECO:0000269|PubMed:26814963}. Cell projection, axon {ECO:0000269|PubMed:26814963}. Cell projection, dendrite {ECO:0000269|PubMed:26814963}. | null | null | null | null | null | FUNCTION: Non-enzymatic component of C3 and C5 convertases and thus essential for the propagation of the classical complement pathway. Covalently binds to immunoglobulins and immune complexes and enhances the solubilization of immune aggregates and the clearance of IC through CR1 on erythrocytes. C4A isotype is respons... | Homo sapiens (Human) |
P0C0L5 | CO4B_HUMAN | MRLLWGLIWASSFFTLSLQKPRLLLFSPSVVHLGVPLSVGVQLQDVPRGQVVKGSVFLRNPSRNNVPCSPKVDFTLSSERDFALLSLQVPLKDAKSCGLHQLLRGPEVQLVAHSPWLKDSLSRTTNIQGINLLFSSRRGHLFLQTDQPIYNPGQRVRYRVFALDQKMRPSTDTITVMVENSHGLRVRKKEVYMPSSIFQDDFVIPDISEPGTWKISARFSDGLESNSSTQFEVKKYVLPNFEVKITPGKPYILTVPGHLDEMQLDIQARYIYGKPVQGVAYVRFGLLDEDGKKTFFRGLESQTKLVNGQSHISLSKAEFQ... | null | null | complement activation [GO:0006956]; complement activation, classical pathway [GO:0006958]; detection of molecule of bacterial origin [GO:0032490]; inflammatory response [GO:0006954]; innate immune response [GO:0045087]; opsonization [GO:0008228]; positive regulation of apoptotic cell clearance [GO:2000427] | axon [GO:0030424]; blood microparticle [GO:0072562]; dendrite [GO:0030425]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; plasma membrane [GO:0005886]; symbiont cell surface [GO:0106139]; synapse [GO:0045202] | carbohydrate binding [GO:0030246]; complement binding [GO:0001848]; endopeptidase inhibitor activity [GO:0004866] | PF00207;PF07703;PF07677;PF01821;PF21145;PF01835;PF17791;PF17789;PF01759;PF07678; | 1.50.10.20;2.20.130.20;2.40.50.120;2.60.120.1540;2.60.40.1930;2.60.40.1940;6.20.50.160;2.60.40.690;1.20.91.20;2.60.40.10; | null | PTM: Prior to secretion, the single-chain precursor is enzymatically cleaved to yield non-identical chains alpha, beta and gamma. During activation, the alpha chain is cleaved by C1 into C4a and C4b, and C4b stays linked to the beta and gamma chains. Further degradation of C4b by C1 into the inactive fragments C4c and ... | SUBCELLULAR LOCATION: Secreted. Synapse {ECO:0000269|PubMed:26814963}. Cell projection, axon {ECO:0000269|PubMed:26814963}. Cell projection, dendrite {ECO:0000269|PubMed:26814963}. | null | null | null | null | null | FUNCTION: Non-enzymatic component of the C3 and C5 convertases and thus essential for the propagation of the classical complement pathway. Covalently binds to immunoglobulins and immune complexes and enhances the solubilization of immune aggregates and the clearance of IC through CR1 on erythrocytes. C4A isotype is res... | Homo sapiens (Human) |
P0C0L7 | PROP_ECOLI | MLKRKKVKPITLRDVTIIDDGKLRKAITAASLGNAMEWFDFGVYGFVAYALGKVFFPGADPSVQMVAALATFSVPFLIRPLGGLFFGMLGDKYGRQKILAITIVIMSISTFCIGLIPSYDTIGIWAPILLLICKMAQGFSVGGEYTGASIFVAEYSPDRKRGFMGSWLDFGSIAGFVLGAGVVVLISTIVGEANFLDWGWRIPFFIALPLGIIGLYLRHALEETPAFQQHVDKLEQGDREGLQDGPKVSFKEIATKYWRSLLTCIGLVIATNVTYYMLLTYMPSYLSHNLHYSEDHGVLIIIAIMIGMLFVQPVMGLLSD... | null | null | amino acid transport [GO:0006865]; cellular hyperosmotic response [GO:0071474]; cellular hyperosmotic salinity response [GO:0071475]; glycine betaine transport [GO:0031460]; osmosensory signaling pathway [GO:0007231]; proline import across plasma membrane [GO:1905647] | plasma membrane [GO:0005886] | proline:proton symporter activity [GO:0005297]; protein homodimerization activity [GO:0042803] | PF08946;PF00083; | 1.20.1250.20; | Major facilitator superfamily, Metabolite:H+ Symporter (MHS) family (TC 2.A.1.6) family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:10026245, ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000255}. | null | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=175 uM for proline {ECO:0000269|PubMed:10026245}; Vmax=83.6 nmol/min/mg enzyme with proline as substrate {ECO:0000269|PubMed:10026245}; | null | null | null | FUNCTION: Proton symporter that senses osmotic shifts and responds by importing osmolytes such as proline, glycine betaine, stachydrine, pipecolic acid, ectoine and taurine. It is both an osmosensor and an osmoregulator which is available to participate early in the bacterial osmoregulatory response. {ECO:0000269|PubMe... | Escherichia coli (strain K12) |
P0C0R5 | PI3R4_RAT | MGNQLAGIAPSQILSVESYFSDIHDFEYDKSLGSTRFFKVARAKHREGLVVVKVFAIQDPTLPLTSYKQELEELKIRLHSAQNCLPFQKAAEKASEKAAMLFRQYVRDNLYDRISTRPFLNNIEKRWIAFQILTAVDQAHKSGVRHGDIKTENVMVTSWNWVLLTDFASFKPTYLPEDNPADFNYFFDTSRRRTCYIAPERFVDGGMFATELEYMRDPSTPLVDLNSNQRTRGELKRAMDIFSAGCVIAELFTEGVPLFDLSQLLAYRNGHFFPEQVLNKIEDRSIRELVTQMIQREPGQRLEADDYLKQQRGNAFPEVF... | 2.7.11.1 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; | autophagosome maturation [GO:0097352]; cellular response to glucose starvation [GO:0042149]; early endosome to late endosome transport [GO:0045022]; late endosome to vacuole transport [GO:0045324]; macroautophagy [GO:0016236]; phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0043491]; phosphatidyl... | autophagosome [GO:0005776]; axoneme [GO:0005930]; late endosome [GO:0005770]; microtubule cytoskeleton [GO:0015630]; nucleus-vacuole junction [GO:0071561]; phosphatidylinositol 3-kinase complex, class III [GO:0035032]; phosphatidylinositol 3-kinase complex, class III, type I [GO:0034271]; phosphatidylinositol 3-kinase ... | ATP binding [GO:0005524]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF00069;PF00400; | 1.25.10.10;1.10.510.10;2.130.10.10; | Protein kinase superfamily, Ser/Thr protein kinase family | PTM: Myristoylated. {ECO:0000250}.; PTM: Probably autophosphorylated. {ECO:0000250}. | SUBCELLULAR LOCATION: Late endosome {ECO:0000250}. Cytoplasmic vesicle, autophagosome {ECO:0000305}. Membrane {ECO:0000250|UniProtKB:Q99570}; Lipid-anchor {ECO:0000250|UniProtKB:Q99570}. Note=As component of the PI3K complex I localized to pre-autophagosome structures. As component of the PI3K complex II localized pred... | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[pr... | null | null | null | null | FUNCTION: Regulatory subunit of the PI3K complex that mediates formation of phosphatidylinositol 3-phosphate; different complex forms are believed to play a role in multiple membrane trafficking pathways: PI3KC3-C1 is involved in initiation of autophagosomes and PI3KC3-C2 in maturation of autophagosomes and endocytosis... | Rattus norvegicus (Rat) |
P0C0R7 | RLME_ECOLI | MTGKKRSASSSRWLQEHFSDKYVQQAQKKGLRSRAWFKLDEIQQSDKLFKPGMTVVDLGAAPGGWSQYVVTQIGGKGRIIACDLLPMDPIVGVDFLQGDFRDELVMKALLERVGDSKVQVVMSDMAPNMSGTPAVDIPRAMYLVELALEMCRDVLAPGGSFVVKVFQGEGFDEYLREIRSLFTKVKVRKPDSSRARSREVYIVATGRKP | 2.1.1.166 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:10748051}; | RNA methylation [GO:0001510] | cytosol [GO:0005829] | rRNA (uridine-2'-O-)-methyltransferase activity [GO:0008650] | PF01728; | 3.40.50.150; | Methyltransferase superfamily, RlmE family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=S-adenosyl-L-methionine + uridine(2552) in 23S rRNA = 2'-O-methyluridine(2552) in 23S rRNA + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:42720, Rhea:RHEA-COMP:10202, Rhea:RHEA-COMP:10203, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:65315, ChEBI:CHEBI:74478; EC=... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.8 uM for 23S rRNA within 50S ribosomal subunits {ECO:0000269|PubMed:12181314}; KM=3.7 uM for S-adenosyl-L-methionine {ECO:0000269|PubMed:12181314}; | null | null | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 55 degrees Celsius. {ECO:0000269|PubMed:12181314}; | FUNCTION: Specifically methylates the uridine in position 2552 of 23S rRNA at the 2'-O position of the ribose in the fully assembled 50S ribosomal subunit. {ECO:0000269|PubMed:10748051}. | Escherichia coli (strain K12) |
P0C0S1 | MSCS_ECOLI | MEDLNVVDSINGAGSWLVANQALLLSYAVNIVAALAIIIVGLIIARMISNAVNRLMISRKIDATVADFLSALVRYGIIAFTLIAALGRVGVQTASVIAVLGAAGLAVGLALQGSLSNLAAGVLLVMFRPFRAGEYVDLGGVAGTVLSVQIFSTTMRTADGKIIVIPNGKIIAGNIINFSREPVRRNEFIIGVAYDSDIDQVKQILTNIIQSEDRILKDREMTVRLNELGASSINFVVRVWSNSGDLQNVYWDVLERIKREFDAAGISFPYPQMDVNFKRVKEDKAA | null | null | intracellular water homeostasis [GO:0009992]; monoatomic ion transmembrane transport [GO:0034220]; protein homooligomerization [GO:0051260] | membrane [GO:0016020]; plasma membrane [GO:0005886] | identical protein binding [GO:0042802]; mechanosensitive monoatomic ion channel activity [GO:0008381] | PF21088;PF05552;PF00924;PF21082; | 1.10.287.1260;2.30.30.60;3.30.70.100; | MscS (TC 1.A.23) family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:10202137, ECO:0000269|PubMed:12551944, ECO:0000269|PubMed:16079137, ECO:0000269|PubMed:23012406, ECO:0000269|PubMed:23074248, ECO:0000269|PubMed:2436228, ECO:0000269|PubMed:7595939}; Multi-pass membrane protein {ECO:0000269|PubMed:12446901, ECO:0000269|PubMe... | null | null | null | null | null | FUNCTION: Mechanosensitive channel that participates in the regulation of osmotic pressure changes within the cell, opening in response to stretch forces in the membrane lipid bilayer, without the need for other proteins. Contributes to normal resistance to hypoosmotic shock. Forms an ion channel of 1.0 nanosiemens con... | Escherichia coli (strain K12) |
P0C0S5 | H2AZ_HUMAN | MAGGKAGKDSGKAKTKAVSRSQRAGLQFPVGRIHRHLKSRTTSHGRVGATAAVYSAAILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGDEELDSLIKATIAGGGVIPHIHKSLIGKKGQQKTV | null | null | cellular response to estradiol stimulus [GO:0071392]; chromatin organization [GO:0006325]; heterochromatin organization [GO:0070828]; positive regulation of transcription by RNA polymerase II [GO:0045944] | euchromatin [GO:0000791]; extracellular exosome [GO:0070062]; heterochromatin [GO:0000792]; nucleosome [GO:0000786]; nucleus [GO:0005634] | chromatin DNA binding [GO:0031490]; nucleosomal DNA binding [GO:0031492]; protein heterodimerization activity [GO:0046982]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; RNA polymerase II core promoter sequence-specific DNA binding [GO:0000979]; structural constituent of chromatin ... | PF00125;PF16211; | 1.10.20.10; | Histone H2A family | PTM: Monoubiquitination of Lys-122 gives a specific tag for epigenetic transcriptional repression. {ECO:0000269|PubMed:11835281}.; PTM: Acetylated on Lys-5, Lys-8, Lys-12 and Lys-14 by KAT2A; KAT2A is recruited by the XPC complex in absence of DNA damage (PubMed:31527837). Acetylated on Lys-5, Lys-8 and Lys-12 during i... | SUBCELLULAR LOCATION: Nucleus. Chromosome. | null | null | null | null | null | FUNCTION: Variant histone H2A which replaces conventional H2A in a subset of nucleosomes. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication... | Homo sapiens (Human) |
P0C0S6 | H2AZ_MOUSE | MAGGKAGKDSGKAKTKAVSRSQRAGLQFPVGRIHRHLKSRTTSHGRVGATAAVYSAAILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGDEELDSLIKATIAGGGVIPHIHKSLIGKKGQQKTV | null | null | cellular response to estradiol stimulus [GO:0071392]; cellular response to insulin stimulus [GO:0032869]; chromatin organization [GO:0006325]; heterochromatin organization [GO:0070828]; positive regulation of transcription by RNA polymerase II [GO:0045944] | euchromatin [GO:0000791]; heterochromatin [GO:0000792]; nucleosome [GO:0000786]; nucleus [GO:0005634] | nucleosomal DNA binding [GO:0031492]; protein heterodimerization activity [GO:0046982]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; RNA polymerase II core promoter sequence-specific DNA binding [GO:0000979]; structural constituent of chromatin [GO:0030527] | PF00125;PF16211; | 1.10.20.10; | Histone H2A family | PTM: Monoubiquitination of Lys-122 gives a specific tag for epigenetic transcriptional repression. {ECO:0000250|UniProtKB:P0C0S5}.; PTM: Acetylated on Lys-5, Lys-8, Lys-12 and Lys-14 by KAT2A; KAT2A is recruited by the XPC complex in absence of DNA damage (By similarity). Acetylated on Lys-5, Lys-8 and Lys-12 during in... | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12660166}. Chromosome {ECO:0000269|PubMed:12660166, ECO:0000269|PubMed:15195148}. Note=Enriched in constitutive heterochromatin (PubMed:12660166, PubMed:15195148). Absent from facultative heterochromatin of the inactive X chromosome (PubMed:12660166). {ECO:0000269|PubMe... | null | null | null | null | null | FUNCTION: Variant histone H2A which replaces conventional H2A in a subset of nucleosomes. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication... | Mus musculus (Mouse) |
P0C0S7 | H2AZ_RAT | MAGGKAGKDSGKAKTKAVSRSQRAGLQFPVGRIHRHLKSRTTSHGRVGATAAVYSAAILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGDEELDSLIKATIAGGGVIPHIHKSLIGKKGQQKTV | null | null | cellular response to estradiol stimulus [GO:0071392]; cellular response to insulin stimulus [GO:0032869]; heterochromatin organization [GO:0070828]; positive regulation of transcription by RNA polymerase II [GO:0045944] | euchromatin [GO:0000791]; heterochromatin [GO:0000792]; nucleosome [GO:0000786]; nucleus [GO:0005634] | chromatin DNA binding [GO:0031490]; nucleosomal DNA binding [GO:0031492]; protein heterodimerization activity [GO:0046982]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; RNA polymerase II core promoter sequence-specific DNA binding [GO:0000979]; structural constituent of chromatin ... | PF00125;PF16211; | 1.10.20.10; | Histone H2A family | PTM: Monoubiquitination of Lys-122 gives a specific tag for epigenetic transcriptional repression. {ECO:0000250|UniProtKB:P0C0S5}.; PTM: Acetylated on Lys-5, Lys-8, Lys-12 and Lys-14 by KAT2A; KAT2A is recruited by the XPC complex in absence of DNA damage (By similarity). Acetylated on Lys-5, Lys-8 and Lys-12 during in... | SUBCELLULAR LOCATION: Nucleus. Chromosome. | null | null | null | null | null | FUNCTION: Variant histone H2A which replaces conventional H2A in a subset of nucleosomes. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication... | Rattus norvegicus (Rat) |
P0C0S8 | H2A1_HUMAN | MSGRGKQGGKARAKAKTRSSRAGLQFPVGRVHRLLRKGNYAERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGKVTIAQGGVLPNIQAVLLPKKTESHHKAKGK | null | null | heterochromatin organization [GO:0070828] | extracellular exosome [GO:0070062]; nucleosome [GO:0000786]; nucleus [GO:0005634] | enzyme binding [GO:0019899]; nucleosomal DNA binding [GO:0031492]; protein heterodimerization activity [GO:0046982]; structural constituent of chromatin [GO:0030527] | PF00125;PF16211; | 1.10.20.10; | Histone H2A family | PTM: Deiminated on Arg-4 in granulocytes upon calcium entry. {ECO:0000269|PubMed:15823041}.; PTM: Monoubiquitination of Lys-120 (H2AK119Ub) by RING1, TRIM37 and RNF2/RING2 complex gives a specific tag for epigenetic transcriptional repression and participates in X chromosome inactivation of female mammals. It is involv... | SUBCELLULAR LOCATION: Nucleus. Chromosome. | null | null | null | null | null | FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is r... | Homo sapiens (Human) |
P0C0S9 | H2A1_BOVIN | MSGRGKQGGKARAKAKTRSSRAGLQFPVGRVHRLLRKGNYAERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGKVTIAQGGVLPNIQAVLLPKKTESHHKAKGK | null | null | heterochromatin organization [GO:0070828] | nucleosome [GO:0000786]; nucleus [GO:0005634] | nucleosomal DNA binding [GO:0031492]; protein heterodimerization activity [GO:0046982]; structural constituent of chromatin [GO:0030527] | PF00125;PF16211; | 1.10.20.10; | Histone H2A family | PTM: Deiminated on Arg-4 in granulocytes upon calcium entry. {ECO:0000250|UniProtKB:P0C0S8}.; PTM: Monoubiquitination of Lys-120 (H2AK119Ub) by RING1, TRIM37 and RNF2/RING2 complex gives a specific tag for epigenetic transcriptional repression and participates in X chromosome inactivation of female mammals. It is invol... | SUBCELLULAR LOCATION: Nucleus. Chromosome. | null | null | null | null | null | FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is r... | Bos taurus (Bovine) |
P0C0T0 | LITAF_RAT | MSAPGPYQAAAGPSVMPTAPPTYEETVGVNSYYPTPPAPQPGPATGLITGPDGKGMNPPSYYTQPVPVPNANAIAVQTVYVQQPISFYDRPIQMCCPSCNKMIVTQLSYNAGALTWLSCGSLCLLGCVAGCCFIPFCVDALQDVDHYCPNCKALLGTYKRL | null | null | cellular response to lipopolysaccharide [GO:0071222]; negative regulation of non-canonical NF-kappaB signal transduction [GO:1901223]; positive regulation of canonical NF-kappaB signal transduction [GO:0043123]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of cytokine production [G... | cytoplasmic side of early endosome membrane [GO:0098559]; cytoplasmic side of late endosome membrane [GO:0098560]; cytoplasmic side of lysosomal membrane [GO:0098574]; cytoplasmic side of plasma membrane [GO:0009898]; extracellular region [GO:0005576]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; lysosoma... | DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; identical protein binding [GO:0042802]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; WW domain binding [GO:0050699]; zinc ion binding [GO:0008270] | PF10601; | null | CDIP1/LITAF family | PTM: Phosphorylated on tyrosine residues in response to EGF. {ECO:0000250|UniProtKB:Q99732}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q99732}. Nucleus {ECO:0000250|UniProtKB:Q99732}. Lysosome membrane {ECO:0000250|UniProtKB:Q99732}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q99732}; Cytoplasmic side {ECO:0000250|UniProtKB:Q99732}. Early endosome membrane {ECO:0000250|UniProtKB:Q99732}. L... | null | null | null | null | null | FUNCTION: Plays a role in endosomal protein trafficking and in targeting proteins for lysosomal degradation. Plays a role in targeting endocytosed EGFR and ERGG3 for lysosomal degradation, and thereby helps down-regulate downstream signaling cascades. Helps recruit the ESCRT complex components TSG101, HGS and STAM to c... | Rattus norvegicus (Rat) |
P0C0T1 | ITPK1_BOVIN | MQTFLKGKRVGYWLSEKKIKKLNFQAFAELCRKRGIEVVQLNLSRPIEEQGPLDVIIHKLTDVILEADQNDSQALELVHRFQEYIDAHPETIVLDPLPAIRTLLDRSKSYELIRKIEAYMKDDRICSPPFMELTSLCGDDTMRLLEENGLAFPFICKTRVAHGTNSHEMAIVFNQEGLSAIQPPCVVQNFINHNAVLYKVFVVGESYTVVQRPSLKNFSAGTSDRESIFFNSHNVSKPESSSVLTALDKIEGVFERPSDEVIRELSRALRQALGVSLFGIDIIINNQTGQHAVIDINAFPGYEGVSEFFTDLLNHIASVL... | 2.7.1.134; 2.7.1.159 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q13572}; Note=Binds 2 magnesium ions per subunit. {ECO:0000250|UniProtKB:Q13572}; | inositol trisphosphate metabolic process [GO:0032957]; necroptotic process [GO:0070266]; neural tube development [GO:0021915]; phosphorylation [GO:0016310] | apical plasma membrane [GO:0016324]; cytoplasm [GO:0005737] | ATP binding [GO:0005524]; hydrolase activity [GO:0016787]; inositol tetrakisphosphate 1-kinase activity [GO:0047325]; inositol tetrakisphosphate 6-kinase activity [GO:0000825]; inositol-1,3,4-trisphosphate 5-kinase activity [GO:0052726]; inositol-1,3,4-trisphosphate 6-kinase activity [GO:0052725]; inositol-3,4,6-trisph... | PF05770;PF17927; | 3.30.1490.220;3.40.50.11370; | ITPK1 family | PTM: Acetylation by EP300 and CREBBP destabilizes ITPK1, and down-regulates enzymatic activity. Deacetylated by SIRT1. {ECO:0000250|UniProtKB:Q13572}. | null | CATALYTIC ACTIVITY: Reaction=1D-myo-inositol 3,4,5,6-tetrakisphosphate + ATP = 1D-myo-inositol 1,3,4,5,6-pentakisphosphate + ADP + H(+); Xref=Rhea:RHEA:12452, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57539, ChEBI:CHEBI:57733, ChEBI:CHEBI:456216; EC=2.7.1.134; Evidence={ECO:0000269|PubMed:8662638}; Physiologica... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=80 nM for Ins(1,3,4)P3 {ECO:0000269|PubMed:8662638}; Vmax=60 nmol/min/mg enzyme with Ins(1,3,4)P3 as substrate {ECO:0000269|PubMed:8662638}; | null | null | null | FUNCTION: Kinase that can phosphorylate various inositol polyphosphate such as Ins(3,4,5,6)P4 or Ins(1,3,4)P3. Phosphorylates Ins(3,4,5,6)P4 at position 1 to form Ins(1,3,4,5,6)P5. This reaction is thought to have regulatory importance, since Ins(3,4,5,6)P4 is an inhibitor of plasma membrane Ca(2+)-activated Cl(-) chan... | Bos taurus (Bovine) |
P0C0T2 | ANKS6_RAT | MGEGALAPGLQLLLRACEQGDTDTARRLLEPGGEPVAGSEAGAEPAGPEAARAVEAGTPVPVDCSDEAGNSALQLAAAGGHEPLVRFLLRRGASVNSRNHYGWSALMQAARCGHASVAHLLLDHGADVNAQNRLGASVLTVASRGGHLGVVKLLLEAGATVDHRNPSGESTASGGSRDELLGITALMAAVQHGHEAVVRLLMEWGADPNHTARTVGWSPLMLAALLGKLSVVQQLVEKGANPDHLGVLEKTAFEVALDRKHRDLADYLDPLTTVRPKTDEEKRRPDIFHALKMGNFQLVKEIADEDPNHVNLVNGDGATP... | null | null | determination of left/right symmetry [GO:0007368]; heart development [GO:0007507]; in utero embryonic development [GO:0001701]; innate immune response [GO:0045087]; kidney development [GO:0001822] | ciliary inversin compartment [GO:0097543]; cytoplasm [GO:0005737]; nucleus [GO:0005634] | identical protein binding [GO:0042802] | PF00023;PF12796;PF00536; | 1.25.40.20;1.10.150.50; | null | PTM: Hydroxylated at Asn-129, most probably by HIF1AN. This hydroxylation results in decreased NEK8-binding. {ECO:0000269|PubMed:23793029}. | SUBCELLULAR LOCATION: Cell projection, cilium {ECO:0000250|UniProtKB:Q6GQX6}. Cytoplasm {ECO:0000269|PubMed:19324013}. Note=Localizes to the proximal region of the primary cilium in the presence of INVS. {ECO:0000250|UniProtKB:Q6GQX6}. | null | null | null | null | null | FUNCTION: Required for renal function. {ECO:0000269|PubMed:16207829}. | Rattus norvegicus (Rat) |
P0C0T4 | RS25B_YEAST | MPPKQQLSKAAKAAAALAGGKKSKKKWSKKSMKDRAQHAVILDQEKYDRILKEVPTYRYVSVSVLVDRLKIGGSLARIALRHLEKEGIIKPISKHSKQAIYTRAAASE | null | null | cytoplasmic translation [GO:0002181] | cytosol [GO:0005829]; cytosolic small ribosomal subunit [GO:0022627] | structural constituent of ribosome [GO:0003735] | PF03297; | 3.30.63.20; | Eukaryotic ribosomal protein eS25 family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:22096102}. | null | null | null | null | null | FUNCTION: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains t... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P0C0T5 | MEPA_ECOLI | MNKTAIALLALLASSASLAATPWQKITQPVPGSAQSIGSFSNGCIVGADTLPIQSEHYQVMRTDQRRYFGHPDLVMFIQRLSSQVSNLGMGTVLIGDMGMPAGGRFNGGHASHQTGLDVDIFLQLPKTRWTSAQLLRPQALDLVSRDGKHVVSTLWKPEIFSLIKLAAQDKDVTRIFVNPAIKQQLCLDAGTDRDWLRKVRPWFQHRAHMHVRLRCPADSLECEDQPLPPSGDGCGAELQSWFEPPKPGTTKPEKKTPPPLPPSCQALLDEHVI | 3.4.24.- | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:15292190}; Note=Binds 2 Zn(2+) ions per subunit. Zn(2+) ion 1 is bound in the active site. Zn(2+) ion 2 is bound at the dimer interface by residues from both subunits. {ECO:0000269|PubMed:15292190}; | peptidoglycan biosynthetic process [GO:0009252]; peptidoglycan metabolic process [GO:0000270]; proteolysis [GO:0006508]; response to xenobiotic stimulus [GO:0009410] | outer membrane-bounded periplasmic space [GO:0030288] | endopeptidase activity [GO:0004175]; metal ion binding [GO:0046872]; metalloendopeptidase activity [GO:0004222]; peptidase activity [GO:0008233]; serine-type endopeptidase activity [GO:0004252] | PF03411; | 3.30.1380.10; | Peptidase M74 family | null | SUBCELLULAR LOCATION: Periplasm {ECO:0000305|PubMed:15292190}. | null | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5-8. {ECO:0000269|PubMed:15292190}; | null | FUNCTION: Murein endopeptidase that cleaves the D-alanyl-meso-2,6-diamino-pimelyl amide bond that connects peptidoglycan strands. Likely plays a role in the removal of murein from the sacculus and could also play a role in the integration of nascent murein strands into the sacculus. {ECO:0000269|PubMed:15292190}. | Escherichia coli (strain K12) |
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